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Mutation of the critical pH-gating residues histidine 231 to glutamate increase open probability of outer membrane protein G in planar lipid bilayer
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作者 Mu Yu peibei sun +4 位作者 Yao He Liang Xiao Demeng sun Longhua Zhang Changlin Tian 《Protein & Cell》 SCIE CSCD 2013年第11期803-806,共4页
Dear Editor,Outer-membrane protein G(OmpG)is a nonspecificβ-barrel porin in the outer membrane of Escherichia coli(E.coli),allowing the passage of ions and molecules up to 900 Da(Fajardo et al.,1998).It comprises of ... Dear Editor,Outer-membrane protein G(OmpG)is a nonspecificβ-barrel porin in the outer membrane of Escherichia coli(E.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 E.coli strains(Nikaido,1999),expres-sion of OmpG was only observed in E.coli mutants lacking OmpF and LamB(Fajardo et al.,1998)to enable the diffu-sion of maltodextrins across the bacte-rial outer membrane.Very 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). 展开更多
关键词 outer planar RESIDUES
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