2f1m

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[[Image:2f1m.gif|left|200px]]
[[Image:2f1m.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_2f1m", creates the "Structure Box" on the page.
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|GENE= acrA, lir, mtcA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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{{STRUCTURE_2f1m| PDB=2f1m | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f1m OCA], [http://www.ebi.ac.uk/pdbsum/2f1m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f1m RCSB]</span>
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'''Conformational flexibility in the multidrug efflux system protein AcrA'''
'''Conformational flexibility in the multidrug efflux system protein AcrA'''
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[[Category: Mikolosko, J.]]
[[Category: Mikolosko, J.]]
[[Category: Zgurskaya, H I.]]
[[Category: Zgurskaya, H I.]]
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[[Category: beta barrel]]
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[[Category: Beta barrel]]
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[[Category: helical hairpin]]
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[[Category: Helical hairpin]]
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[[Category: lipoyl domain]]
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[[Category: Lipoyl domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:21:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:56:45 2008''
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Revision as of 00:21, 4 May 2008

Template:STRUCTURE 2f1m

Conformational flexibility in the multidrug efflux system protein AcrA


Overview

Intrinsic resistance to multiple drugs in many gram-negative bacterial pathogens is conferred by resistance nodulation cell division efflux pumps, which are composed of three essential components as typified by the extensively characterized Escherichia coli AcrA-AcrB-TolC system. The inner membrane drug:proton antiporter AcrB and the outer membrane channel TolC export chemically diverse compounds out of the bacterial cell, and require the activity of the third component, the periplasmic protein AcrA. The crystal structures of AcrB and TolC have previously been determined, and we complete the molecular picture of the efflux system by presenting the structure of a stable fragment of AcrA. The AcrA fragment resembles the elongated sickle shape of its homolog Pseudomonas aeruginosa MexA, being composed of three domains: beta-barrel, lipoyl, and alpha-helical hairpin. Notably, unsuspected conformational flexibility in the alpha-helical hairpin domain of AcrA is observed, which has potential mechanistic significance in coupling between AcrA conformations and TolC channel opening.

About this Structure

2F1M is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Conformational flexibility in the multidrug efflux system protein AcrA., Mikolosko J, Bobyk K, Zgurskaya HI, Ghosh P, Structure. 2006 Mar;14(3):577-87. PMID:16531241 Page seeded by OCA on Sun May 4 03:21:23 2008

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