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[[ | ==Crystal Structure of the Periplasmic Catecholate-Siderophore Binding Protein VctP from Vibrio Cholerae== | ||
<StructureSection load='3tef' size='340' side='right' caption='[[3tef]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3tef]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TEF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TEF FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VC_A0227 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=666 Vibrio cholerae])</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tef OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tef RCSB], [http://www.ebi.ac.uk/pdbsum/3tef PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
VctP, one of the two essential siderophore-binding PBPs from the pathogen Vibrio cholerae, plays an important role in the transport of enterobactin and vibriobactin, which have quite different configurations of iron coordination, from the periplasm to the inner membrane. The current study reports the crystal structure of VctP from V. cholerae N16961 at 1.7A resolution. A structural comparison of VctP with its homologues and the results of molecular docking indicate that enterobactin and vibriobactin share the same binding pocket. Significantly, a basic triad consisting of Arg137, Arg226 and Arg270 is used to balance the three negative charges of ferric-enterobactin, while a basic dyad consisting of Arg137 and Arg270 is used to balance the two negative charges of ferric-vibriobactin. | |||
Crystal structure of periplasmic catecholate-siderophore binding protein VctP from Vibrio cholerae at 1.7 A resolution.,Liu X, Du Q, Wang Z, Liu S, Li N, Chen Y, Zhu C, Zhu D, Wei T, Huang Y, Xu S, Gu L FEBS Lett. 2012 Apr 24;586(8):1240-4. Epub 2012 Mar 28. PMID:22575663<ref>PMID:22575663</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
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[[Category: Vibrio cholerae]] | [[Category: Vibrio cholerae]] | ||
[[Category: Chen, Y.]] | [[Category: Chen, Y.]] | ||
Revision as of 12:14, 11 June 2014
Crystal Structure of the Periplasmic Catecholate-Siderophore Binding Protein VctP from Vibrio CholeraeCrystal Structure of the Periplasmic Catecholate-Siderophore Binding Protein VctP from Vibrio Cholerae
Structural highlights
Publication Abstract from PubMedVctP, one of the two essential siderophore-binding PBPs from the pathogen Vibrio cholerae, plays an important role in the transport of enterobactin and vibriobactin, which have quite different configurations of iron coordination, from the periplasm to the inner membrane. The current study reports the crystal structure of VctP from V. cholerae N16961 at 1.7A resolution. A structural comparison of VctP with its homologues and the results of molecular docking indicate that enterobactin and vibriobactin share the same binding pocket. Significantly, a basic triad consisting of Arg137, Arg226 and Arg270 is used to balance the three negative charges of ferric-enterobactin, while a basic dyad consisting of Arg137 and Arg270 is used to balance the two negative charges of ferric-vibriobactin. Crystal structure of periplasmic catecholate-siderophore binding protein VctP from Vibrio cholerae at 1.7 A resolution.,Liu X, Du Q, Wang Z, Liu S, Li N, Chen Y, Zhu C, Zhu D, Wei T, Huang Y, Xu S, Gu L FEBS Lett. 2012 Apr 24;586(8):1240-4. Epub 2012 Mar 28. PMID:22575663[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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