Mutation of the critical pH-gating residues histidine 231 to glutamate increase open probability of outer membrane protein G in planar lipid bilayer

作     者：Mu Yu Peibei Sun Yao He Liang Xiao Demeng Sun Longhua Zhang Changlin Tian 

作者机构：High Magnetic Field LaboratoryChinese Academic of SciencesHefei 230031China Hefei National Laboratory for Physical Science at Microscale and School of Life ScienceUniversity of Science and Technology of ChinaHefei 230027China 

出 版 物：《Protein & Cell》 (蛋白质与细胞（英文版）)

年 卷 期：2013年第4卷第11期

页      面：803-806页

核心收录：

学科分类：0710[理学-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] 070303[理学-有机化学] 0703[理学-化学] 

基　　金：supported by the National Basic Research Program (973 Program) the National Natural Science Foundation of China to C.T the National Natural Science Foundation of China to L.Z 

主　　题：outer planar residues 

摘      要：Dear Editor,Outer-membrane protein G(OmpG)is a nonspecificβ-barrel porin in the outer membrane of Escherichia coli(***),allowing the passage of ions and molecules up to 900 Da(Fajardo et al.,1998).It comprises of 280 amino acids that form 14-strandedβ-sheets with seven long loops(L1-L7)on the extra-cellular side and six short turns on the periplasmic side(Subbarao and van den Berg,2006;Yildiz et al.,2006;Liang and Tamm,2007).Despite that the OmpG gene exists in the genome of several *** strains(Nikaido,1999),expres-sion of OmpG was only observed in *** mutants lacking OmpF and LamB(Fajardo et al.,1998)to enable the diffu-sion of maltodextrins across the bacte-rial outer *** interestingly,unlike usual trimeric channel-forming porins,OmpG exhibits fascinating characteristics of a functional monomer in physiological and structural studies(Conlan and Bayley,2003;Mari et al.,2010).