Structure of protein O-mannose kinase reveals a unique active site architecture
作者单位：The State Key Laboratory of Protein and Plant Gene ResearchSchool of Life SciencesAcademy for Advanced Interdisciplinary StudiesPeking-Tsinghua Center for Life SciencesPeking University Howard Hughes Medical InstituteDepartment of Molecular Physiology and BiophysicsDepartment of NeurologyDepartment of Internal MedicineUniversity of Iowa Roy J.and Lucille A.Carver College of Medicine National Institute of Biological SciencesBeijing Department of BiophysicsUniversity of TexasSouthwestern Medical Center Beijing National Laboratory for Molecular SciencesCollege of Chemistry and Molecular EngineeringPeking-Tsinghua Center for Life SciencesSynthetic and Functional Biomolecules CenterKey Laboratory of Bioorganic Chemistry and Molecular Engineering of Ministry of EducationPeking University Medical Nuclear Magnetic Resonance FacilityUniversity of Iowa Roy J.and Lucille A.Carver College of Medicine Department of PharmacologyDepartment of Cellular and Molecular MedicineDepartment of Chemistry and BiochemistryUniversity of California
会议名称：《中国晶体学会第六届学术年会暨会员代表大会（大分子晶体学分会）》
会议日期：2016年
学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术]
摘 要：ThepseudokinaseSg K196 is a protein O-mannose kinase(POMK)that catalyzes an essential phosphorylation step during biosynthesis of the laminin-binding glycan ***,the catalytic mechanism underlying this activity remains *** we present the crystal structure of Danio rerio POMK in complex with Mg ions,ADP,aluminum fluoride,and