4k7q: Difference between revisions

Revision as of 11:44, 30 November 2022

Crystal Structure of AcrB Complexed with Linezolid at 3.5 Resolution

Structural highlights

4k7q is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	ZLD
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACRB_ECOLI AcrAB is a drug efflux protein with a broad substrate specificity.^[1] ^[2] ^[3]

Publication Abstract from PubMed

AcrB is an inner membrane resistance-nodulation-cell division efflux pump and is part of the AcrAB-TolC tripartite efflux system. We have determined the crystal structure of AcrB with bound Linezolid at a resolution of 3.5 A. The structure shows that Linezolid binds to the A385/F386 loops of the symmetric trimer of AcrB. A conformational change of a loop in the bottom of the periplasmic cleft is also observed.

Crystal structure of AcrB complexed with linezolid at 3.5 A resolution.,Hung LW, Kim HB, Murakami S, Gupta G, Kim CY, Terwilliger TC J Struct Funct Genomics. 2013 Jun;14(2):71-5. doi: 10.1007/s10969-013-9154-x., Epub 2013 May 15. PMID:23673416^[4]

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

References

↑ Murakami S, Nakashima R, Yamashita E, Matsumoto T, Yamaguchi A. Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature. 2006 Sep 14;443(7108):173-9. Epub 2006 Aug 16. PMID:16915237 doi:10.1038/nature05076
↑ Seeger MA, Schiefner A, Eicher T, Verrey F, Diederichs K, Pos KM. Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. Science. 2006 Sep 1;313(5791):1295-8. PMID:16946072 doi:313/5791/1295
↑ Sennhauser G, Amstutz P, Briand C, Storchenegger O, Grutter MG. Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors. PLoS Biol. 2007 Jan;5(1):e7. PMID:17194213 doi:10.1371/journal.pbio.0050007
↑ Hung LW, Kim HB, Murakami S, Gupta G, Kim CY, Terwilliger TC. Crystal structure of AcrB complexed with linezolid at 3.5 A resolution. J Struct Funct Genomics. 2013 Jun;14(2):71-5. doi: 10.1007/s10969-013-9154-x., Epub 2013 May 15. PMID:23673416 doi:10.1007/s10969-013-9154-x

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OCA

[1] Murakami S, Nakashima R, Yamashita E, Matsumoto T, Yamaguchi A. Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature. 2006 Sep 14;443(7108):173-9. Epub 2006 Aug 16. PMID:16915237 doi:10.1038/nature05076

[2] Seeger MA, Schiefner A, Eicher T, Verrey F, Diederichs K, Pos KM. Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. Science. 2006 Sep 1;313(5791):1295-8. PMID:16946072 doi:313/5791/1295

[3] Sennhauser G, Amstutz P, Briand C, Storchenegger O, Grutter MG. Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors. PLoS Biol. 2007 Jan;5(1):e7. PMID:17194213 doi:10.1371/journal.pbio.0050007

[4] Hung LW, Kim HB, Murakami S, Gupta G, Kim CY, Terwilliger TC. Crystal structure of AcrB complexed with linezolid at 3.5 A resolution. J Struct Funct Genomics. 2013 Jun;14(2):71-5. doi: 10.1007/s10969-013-9154-x., Epub 2013 May 15. PMID:23673416 doi:10.1007/s10969-013-9154-x

[1]

[2]

[3]

[4]

@@ Line 1: / Line 1: @@
 ==Crystal Structure of AcrB Complexed with Linezolid at 3.5 Resolution==
-<StructureSection load='4k7q' size='340' side='right' caption='[[4k7q]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
+<StructureSection load='4k7q' size='340' side='right'caption='[[4k7q]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4k7q]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K7Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K7Q FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4k7q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K7Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K7Q FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZLD:N-{[(5S)-3-(3-FLUORO-4-MORPHOLIN-4-YLPHENYL)-2-OXO-1,3-OXAZOLIDIN-5-YL]METHYL}ACETAMIDE'>ZLD</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZLD:N-{[(5S)-3-(3-FLUORO-4-MORPHOLIN-4-YLPHENYL)-2-OXO-1,3-OXAZOLIDIN-5-YL]METHYL}ACETAMIDE'>ZLD</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">acrB, acrE, b0462, JW0451 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4k7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k7q OCA], [https://pdbe.org/4k7q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k7q RCSB], [https://www.ebi.ac.uk/pdbsum/4k7q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k7q ProSAT]</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=4k7q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k7q OCA], [http://pdbe.org/4k7q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k7q RCSB], [http://www.ebi.ac.uk/pdbsum/4k7q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k7q ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ACRB_ECOLI ACRB_ECOLI]] AcrAB is a drug efflux protein with a broad substrate specificity.<ref>PMID:16915237</ref> <ref>PMID:16946072</ref> <ref>PMID:17194213</ref>
+[https://www.uniprot.org/uniprot/ACRB_ECOLI ACRB_ECOLI] AcrAB is a drug efflux protein with a broad substrate specificity.<ref>PMID:16915237</ref> <ref>PMID:16946072</ref> <ref>PMID:17194213</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
-[[Category: Gupta, G]]
+[[Category: Large Structures]]
-[[Category: Hung, L W]]
+[[Category: Gupta G]]
-[[Category: Kim, C Y]]
+[[Category: Hung LW]]
-[[Category: Kim, H B]]
+[[Category: Kim CY]]
-[[Category: Murakami, S]]
+[[Category: Kim HB]]
-[[Category: Terwilliger, T C]]
+[[Category: Murakami S]]
-[[Category: Inner membrane resistance-nodulation-cell division efflux pump]]
+[[Category: Terwilliger TC]]
-[[Category: Membrane protein-antibiotic complex]]

4k7q: Difference between revisions

Revision as of 11:44, 30 November 2022

Crystal Structure of AcrB Complexed with Linezolid at 3.5 Resolution

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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