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Protein & Cell 2012年第12期3卷 893-902页

作者： yuna sun Yu Guo Zhiyong Lou National Laboratory of Macromolecules Institute of BiophysicsChinese Academy of ScienceBeijing 100101China Laboratory of Structural Biology and MOE Laboratory of Protein Science School of Medicine and Life SciencesTsinghua UniversityBeijing 100084China High-throughput Molecular Drug Discovery Center Tianjin Joint Academy of Biomedicine and TechnologyTianjin 300457China College of Pharmacy and State Key Laboratory of Medicinal Chemical Biology Nankai UniversityTianjin 300071China

Nucleocapsid protein(NPs)of negative-sense single-stranded RNA(-ssRNA)viruses function in different stages of viral replication,transcription,and *** investigations show that-ssRNA viruses that encode NPs preliminarily serve as structural building blocks that encapsidate and protect the viral genomic RNA and mediate the interaction between genomic RNA and RNA-dependent RNA ***,recent structural results have revealed other bio-logical functions of-ssRNA viruses that extend our understanding of the versatile roles of virally encoded NPs.

关键词： -ssRNA virus nucleocapsid protein crystal structure function

Catalogue of Eucnemidae(Coleoptera: Elateroidea) in China

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Zoological Systematics 2020年第4期45卷 290-311页

作者： Ziye Meng Xiaoqin Chen yuna sun Yongying Ruan Shihong Jiang Research Center of Buckwheat Industry Technology Guizhou Normal UniversityGuiyangGuizhou 550001China College of Applied Chemistry and Biotechnology Shenzhen PolytechnicShenzhenGuangdong 518055China School of Foreign Languages Guizhou Normal UniversityGuiyangGuizhou 550001China

This catalogue records the Eucnemidae species in China,including 15 genera,namely Isorhipis Lacordaire,1835,Melasis Olivier,1790,Calyptocerus Guérin-Méneville,1843,Hylis Gozis,1886,Epiphanis Eschscholtz,1829,Farsus Jacquelin du Val,1860,Microrhagus Dejean,1833,Dyscharachthis Blackburn,1900,Galbites Fleutiaux,1918,Procladidus Fleutiaux,1921,Pseudochapianus Lucht,1987,Raapia Fleutiaux,1899,Scython Laporte,1835,Serrifornax Fleutiaux,1926,Fornax Laporte,1835 and 25 species,belonging to 3 subfamilies:Melasinae,Eucneminae,and Macraulacinae,*** taxonomy in the catalogue is based on the present classification system follows Muona.

关键词： Eucnemidae false click beetles checklist China

Crystal structure of a secreted lipase from Gibberella zeae reveals a novel “double-lock” mechanism

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Protein & Cell 2010年第8期1卷 760-770页

作者： Zhiyong Lou Ming Li yuna sun Ye Liu Zheng Liu Wenping Wu Zihe Rao Laboratory of Structural Biology Tsinghua UniversityBeijing 100084China Novozymes China 14 Xinxi LuShangdi ZoneHaidian DistrictBeijing 100085China National Laboratory of Biomacromolecules Institute of BiophysicsChinese Academy of SciencesBeijing 100101China

Fusarium graminearum(sexual stage:Gibberella zeae)is the causative agent of Fusarium Head Blight(FHB),which is one of the most destructive plant disease of cereals,accounting for high grain yield losses,especially for wheat and *** other fungal pathogens,several extracellular enzymes secreted by *** are known to be involved in host *** these secreted lipases,*** lipase(GZEL),which is encoded by the FGL1 gene,was demonstrated to be crucial to *** ***,the precise mechanism of GZEL remains unclear due to a lack of detailed structural *** this study,we report the crystal structure of GZEL at the atomic *** structure of GZEL displays distinct structural differences compared to reported homologues and indicates a unique“double lock”enzymatic *** gain insight into substrate/inhibitor recognition,we proposed a model of GZEL in complex with substrate and the lipase inhibitor ebelactone B(based on the reported structures of GZEL homologues),which defines possible substrate binding sites within the catalytic cleft and suggests an“anti sn-l”binding *** results pave the way to elucidating the mechanism of GZEL and thus provide clues for the design of anti-FHB inhibitors.

关键词： lipase Gibberella zeae crystal structure mechanism inhibitor

Molecular basis for the inhibition of β-hydroxyacyI-ACP dehydratase HadAB complex from Mycobacterium tuberculosis by flavonoid inhibitors

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Protein & Cell 2015年第7期6卷 504-517页

作者： Yu Dong Xiaodi Qiu Neil Shaw Yueyang Xu yuna sun Xuemei Li Jun Li Zihe Rao National Laboratory of Biomacromolecules Institute of Biophysics Chinese Academy of Sciences Beijing 100101 China University of Chinese Academy of Sciences Beijing 100049China Structure Biology Laboratory Tsinghua University Beijing 100084 China Tianjin Key Laboratory of Protein Science College of'Life Sciences Nankai University Tianjin 300071 China

Dehydration is one of the key steps in the biosynthesis of mycolic acids and is vital to the growth of Mycobac- terium tuberculosis （Mtb）. Consequently, stalling dehy-dration cures tuberculosis （TB）. Clinically used anti-TB drugs like thiacetazone （TAC） and isoxyl （ISO） as well as flavonoids inhibit the enzyme activity of the β-hydroxy- acyI-ACP dehydratase HadAB complex. How this inhi- bition is exerted, has remained an enigma for years. Here, we describe the first crystal structures of the MtbHadAB complex bound with flavonoid inhibitor butein, 2＇,4,4＇-trihydroxychalcone or fisetin. Despite sharing no sequence identity from Blast, HadA and HadB adopt a very similar hotdog fold. HadA forms a tight dimer with HadB in which the proteins are sitting side-by-side, but are oriented anti-parallel. While HadB contributes the catalytically critical His-Asp dyad, HadA binds the fatty acid substrate in a long channel. The atypical double hotdog fold with a single active site formed by MtbHadAB gives rise to a long, narrow cavity that vertically traverses the fatty acid binding channel. At the base of this cavity lies Cys61, which upon muta- tion to Ser confers drug-resistance in TB patients. We show that inhibitors bind in this cavity and protrude into the substrate binding channel. Thus, inhibitors of MtbHadAB exert their effect by occluding substrate from the active site, The unveiling of this mechanism of inhibition paves the way for accelerating development of next generation of anti-TB drugs,

关键词： Mycobacterium tuberculosis hotdog fold,mycolic acid dehydratase flavonoid thiacetazone isoxyl

A novel non-radioactive assay for HIV-RT(RdDp)based on pyrosequencing for high-throughput drug screening

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Protein & Cell 2010年第3期1卷 284-290页

作者： Chang Zhang Yang Wu yuna sun Chuan Hong Kehui Xiang Yu Guo Mark Bartlam Zhiyong Lou Tsinghua-Nankai-IBP Joint Research Group for Structural Biology Tsinghua UniversityBeijing 100084China National Laboratory of Macromolecules Institute of BiophysicsChinese Academy of SciencesBeijing 100101China College of Life Sciences and Tianjin State Laboratory of Protein Sciences Nankai UniversityTianjin 300071China

Current in vitro assays for the activity of HIV-RT(reverse transcriptase)require radio-labeled or chemically modified nucleotides to detect reaction ***,these assays are inherently end-point measurements and labor *** we describe a novel non-radioactive assay based on the principle of pyrosequencing coupledenzyme system to monitor the activity of HIV-RT by indirectly measuring the release of pyrophosphate(PPi),which is generated during nascent strand *** results show that our assay could monitor HIV-RT activity with high sensitivity and is suitable for rapid highthroughput drug screening targeting anti-HIV therapies due to its high speed and ***,this assay can be used to measure primase activity in an easy and sensitive manner,which suggests that this novel approach could be wildly used to analyze the activity of PPi-generated and ATP-free enzyme reactions.

关键词： HIV-RT(RdDp) assay non-radioactive high throughput drug screening

Structural basis for mechanochemical role of Arabidopsis thaliana dynamin-related protein in membrane fission

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Journal of Molecular Cell Biology 2011年第6期3卷 378-381页

作者： Liming Yan Yuanyuan Ma yuna sun Jian Gao Xiaoyue Chen Jiewei Liu Congwan Wang Zihe Rao Zhiyong Lou Laboratory of Structural Biology and MOE Laboratory of Protein Science School of MedicineTsinghua UniversityBeijing 100084China College of Life Sciences and Tianjin State Laboratory of Protein Science Nankai UniversityTianjin 300071China National Laboratory of Macromolecules Institute of BiophysicsChinese Academy of ScienceBeijing 100101China Beijing 107 Middle School BeijingChina

Dear Editor,Dynamins and dynamin-related proteins(DRPs)constitute a large superfamily of GTPases throughout animal,plant,and bacteria and play essential roles in core cellular processes(Praefcke and McMahon,2004).Plant specific dynamin-related subfamilies share essential functions with those in mammalian cell,***mediated endocytosis and fission of mitochondria.

关键词： chemical families constitute

A structural view of the antibiotic degradation enzyme NDM-1 from a superbug

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Protein & Cell 2011年第5期2卷 384-394页

作者： Yu Guo Jing Wang Guojun Niu Wenqing Shui yuna sun Honggang Zhou Yaozhou Zhang Cheng Yang Zhiyong Lou Zihe Rao High-throughput Molecular Drug Discovery Center Tianjin Joint Academy of Biotechnology and MedicineTianjin 300071China Laboratory of Structural Biology Tsinghua UniversityBeijing 100084China College of Life Science Nankai UniversityTianjin 300074China National Laboratory of Macromolecules Institute of BiophysicsChinese Academy of SciencesBeijing 100101China

Gram-negative Enterobacteriaceae with resistance to carbapenem conferred by New Delhi metallo-β-lactamase 1(NDM-1)are a type of newly discovered antibioticresistant *** rapid pandemic spread of NDM-1 bacteria worldwide(spreading to India,Pakistan,Europe,America,and Chinese Taiwan)in less than 2 months characterizes these microbes as a potentially major global health *** drug resistance of NDM-1 bacteria is largely due to plasmids containing the blaNDM-1 gene shuttling through bacterial *** NDM-1 enzyme encoded by the blaNDM-1 gene hydrolyzes β-lactam antibiotics,allowing the bacteria to escape the action of *** the biological functions and structural features of NDM-1 have been proposed according to results from functional and structural investigation of its homologues,the precise molecular characteristics and mechanism of action of NDM-1 have not been ***,we report the threedimensional structure of NDM-1 with two catalytic zinc ions in its active *** and mass spectroscopy results revealed that D-captopril can effectively inhibit the enzymatic activity of NDM-1 by binding to its active site with high binding *** unique features concerning the primary sequence and structural conformation of the active site distinguish NDM-1 from other reported metallo-β-lactamases(MBLs)and implicate its role in wide spectrum drug *** also discuss the molecular mechanism of NDM-1 action and its essential role in the pandemic of drug-resistant NDM-1 *** results will provide helpful information for future drug discovery targeting drug resistance caused by NDM-1 and related metallo-β-lactamases.

关键词： New Delhi metallo-β-lactamase 1(NDM-1) drug resistance crystal structure drug discovery

Molecular mechanism of SCARB2-mediatec attachment and uncoating of EV71

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Protein & Cell 2014年第9期5卷 692-703页

作者： Minghao Dang Xiangxi Wang Quan Wang Yaxin Wang Jianping Lin yuna sun Xuemei Li Liguo Zhang Zhiyong Lou Junzhi Wang Zihe Rao National Laboratory of Macromolecules Institute of Biophysics Chinese Academy of Science Beijing 100101 China Laboratory of Structural Biology School of Medicine Tsinghua University Beijing 100084 China School of Life Sciences School of Pharmacy Nankai University Tianjin 300071 China National Institutes for Food and Drug Control Beijing 100050 China

Unlike the well-established picture for the entry of enveloped viruses, the mechanism of cellular entry of non-enveloped eukaryotic viruses remains largely mysterious. Picornaviruses are representative models for such viruses, and initiate this entry process by their functional receptors. Here we present the structural and functional studies of SCARB2, a functional receptor of the important human enterovirus 71 （EV71）. SCARB2 is responsible for attachment as well as uncoating of EV71. Differences in the structures of SCARB2 under neutral and acidic conditions reveal that SCARB2 undergoes a pivotal pH-dependent conformational change which opens a lipid-transfer tunnel to mediate the expulsion of a hydrophobic pocket factor from the virion, a pre-requisite for uncoating. We have also identified the key residues essential for attachment to SCARB2, identifying the canyon region of EV71 as mediating the receptor interaction. Together these results provide a clear understanding of cellular attachment and initiation of uncoating for enteroviruses.

关键词： viral entry uncoating picornavirusesreceptor binding SCARB2 EV71 lipid transfer tunnel

The nucleoprotein of severe fever with thrombocytopenia syndrome virus processes a stable hexameric ring to facilitate RNA encapsidation

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Protein & Cell 2013年第6期4卷 445-455页

作者： Honggang Zhou yuna sun Ying Wang Min Liu Chao Liu Wenming Wang Xiang Liu Le Li Fei Deng Hualin Wang Yu Guo Zhiyong Lou College of Pharmacy and State Key Laboratory of Medicinal Chemical Biology Nankai UniversityTianjin 300071China Laboratory of Structural Biology and MOE Laboratory of Protein Science School of Medicine and Life SciencesTsinghua UniversityBeijing 100084China State Key Laboratory of Virology Wuhan Institute of VirologyChinese Academy of SciencesWuhan 430071China National Laboratory of Macromolecules Institute of BiophysicsChinese Academy of ScienceBeijing 100101China High-throughput Molecular Drug Discovery Center Tianjin Joint Academy of Biotechnology and MedicineTianjin 300457China

Severe fever with thrombocytopenia syndrome virus(SFTSV),a member of the Phlebovirus genus from the Bunyaviridae family endemic to China,is the causative agent of life-threatening severe fever with thrombocyto-penia syndrome(SFTS),which features high fever and *** to other negative-sense RNA viruses,SFTSV encodes a nucleocapsid protein(NP)that is essen-tial for viral *** facilitates viral RNA encapsida-tion and is responsible for the formation of ribonucleopro-tein ***,recent studies have indicated that NP from Phlebovirus members behaves in inhomogene-ous oligomerization *** the present study,we report the crystal structure of SFTSV NP at 2.8Åresolution and demonstrate the mechanism by which it processes a ring-shaped hexameric form to accomplish RNA *** residues essential for oligomerization are identi-fi ed through mutational analysis and identifi ed to have a signifi cant impact on RNA binding,which suggests that correct formation of highly ordered oligomers is a criti-cal step in RNA *** fi ndings of this work provide new insights into the discovery of new antiviral reagents for Phlebovirus infection.

关键词： SFTSV nucleoprotein oligomer RNP as-sembly crystal structure

A comprehensive procedure for antiviral inhibitor discovery using EV71 as an example

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Biophysics Reports 2015年第2期1卷 81-89页

作者： Lin Cao Shouhai Zhu Yaxin Wang Zhiyong Lou yuna sun College of Biotechnology Tianjin University of Science and Technology National Laboratory of Macromolecules Institute of Biophysics Chinese Academy of Science Laboratory of Structural Biology School of Medicine Tsinghua University

The prevalence of chronic viral infectious diseases, the emergence and re-emergence of new viral infections, and in particular, resistance to currently used antiviral drugs have led to increased demand for new antiviral strategies and reagents. Increased understanding of the molecular mechanisms of viral infection has provided great potential for the discovery of new antiviral agents that target viral proteins or host factors. In this work, we introduce a comprehensive system using enteroviruses 71(EV71) as an example for leading compound discovery to develop new antiviral.

关键词： Antiviral Assay Entry Replication Virus