期刊
FEBS LETTERS
卷 581, 期 22, 页码 4217-4222出版社
WILEY
DOI: 10.1016/j.febslet.2007.07.069
关键词
homology modelling; P-glycoprotein; MalK; nucleotide catalytic cycle; ABC transporter; multidrug; resistance; Staphylococcus aureus ABC transporter
We exploit the biochemical and sequence similarity between Staphylococcus aureus Sav1866 and P-glycoprotein to develop a homology model of P-glycoprotein representing an ATP-bound state, which captures the major features of the low-resolution EM structure and is consistent with cysteine mutagenesis studies. Using insights from the MalK crystal structures and BtuCD simulations, we model two nucleotide-free conformations. Conformational changes are characterized by pincering rigid-body rotations of the nucleotide-binding domains, inducing transmembrane domain reorganizations which correspond to the two lowest frequency normal modes of the protein. These conformations (see supplementary material) may characterize some of the major steps in the nucleotide catalytic cycle. (c) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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