2f1m

From Proteopedia

(Difference between revisions)

Revision as of 07:32, 18 October 2017

Conformational flexibility in the multidrug efflux system protein AcrA

Structural highlights

2f1m is a 4 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. The November 2007 RCSB PDB Molecule of the Month feature on Multidrug Resistance Transporters by David S. Goodsell is 10.2210/rcsb_pdb/mom_2007_11. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:	acrA, lir, mtcA ("Bacillus coli" Migula 1895)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ACRA_ECOLI] AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates. This subunit may act as an adapter protein that links AcrB and TolC stably together. It is elongated in shape, being long enough to span the periplasm.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zgurskaya HI, Nikaido H. AcrA is a highly asymmetric protein capable of spanning the periplasm. J Mol Biol. 1999 Jan 8;285(1):409-20. PMID:9878415 doi:http://dx.doi.org/10.1006/jmbi.1998.2313
↑ Mikolosko J, Bobyk K, Zgurskaya HI, Ghosh P. Conformational flexibility in the multidrug efflux system protein AcrA. Structure. 2006 Mar;14(3):577-87. PMID:16531241 doi:10.1016/j.str.2005.11.015

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2f1m"

@@ Line 1: / Line 1: @@
 ==Conformational flexibility in the multidrug efflux system protein AcrA==
 <StructureSection load='2f1m' size='340' side='right' caption='[[2f1m]], [[Resolution|resolution]] 2.71&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">acrA, lir, mtcA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2f1m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2f1m RCSB], [http://www.ebi.ac.uk/pdbsum/2f1m PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/2f1m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2f1m RCSB], [http://www.ebi.ac.uk/pdbsum/2f1m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2f1m ProSAT]</span></td></tr>
 </table>
 == Function ==

2f1m

From Proteopedia

Revision as of 07:32, 18 October 2017

Conformational flexibility in the multidrug efflux system protein AcrA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox