کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2029994 | 1071009 | 2010 | 11 صفحه PDF | دانلود رایگان |

SummaryOriginally described in bacteria, drug transporters are now recognized as major determinants in antibiotics resistance. For Gram-negative bacteria, the reversible assembly consisting of an inner membrane protein responsible for the active transport, a periplasmic protein, and an exit outer membrane channel achieves transport. The opening of the outer membrane protein OprM from Pseudomonas aeruginosa was modeled through normal mode analysis starting from a new X-ray structure solved at 2.4 Å resolution in P212121 space group. The three monomers are not linked by internal crystallographic symmetries highlighting the possible functional differences. This structure is closed at both ends, but modeling allowed for an opening that is not reduced to the classically proposed “iris-like mechanism.”
Graphical AbstractFigure optionsDownload high-quality image (240 K)Download as PowerPoint slideHighlights
► A trimer OprM protein structure without three-fold crystallographic axis
► Model of OprM opening by normal mode analysis
Journal: - Volume 18, Issue 4, 14 March 2010, Pages 507–517