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==2.2A resolution structure of Holo hemophore HasA from Yersinia pestis== | |||
<StructureSection load='4jet' size='340' side='right' caption='[[4jet]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4jet]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JET OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JET FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jer|4jer]], [[4jes|4jes]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hasA, y0314, YP_3127, YPO3922 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=632 Yersinia pestis])</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=4jet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jet OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jet RCSB], [http://www.ebi.ac.uk/pdbsum/4jet PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Hemophores from Serratia marcescens (HasAsm) and Pseudomonas aeruginosa (HasAp) bind hemin between two loops, which harbor the axial ligands H32 and Y75. Hemin binding to the Y75 loop triggers closing of the H32 loop and enables binding of H32. Because Yersinia pestis HasA (HasAyp) presents a Gln at position 32, we determined the structures of apo- and holo-HasAyp. Surprisingly, the Q32 loop in apo-HasAyp is already in the closed conformation, but no residue from the Q32 loop binds hemin in holo-HasAyp. In agreement with the minimal reorganization between the apo- and holo-structures, the hemin on-rate is too fast to detect by conventional stopped-flow measurements. | |||
The Hemophore HasA from Yersinia pestis (HasAyp) Coordinates Hemin with a Single Residue, Tyr75, and with Minimal Conformational Change.,Kumar R, Lovell S, Matsumura H, Battaile KP, Moenne-Loccoz P, Rivera M Biochemistry. 2013 Apr 23;52(16):2705-7. doi: 10.1021/bi400280z. Epub 2013 Apr, 11. PMID:23578210<ref>PMID:23578210</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Yersinia pestis]] | [[Category: Yersinia pestis]] | ||
[[Category: Battaile, K P | [[Category: Battaile, K P]] | ||
[[Category: Kumar, R | [[Category: Kumar, R]] | ||
[[Category: Lovell, S | [[Category: Lovell, S]] | ||
[[Category: Rivera, M | [[Category: Rivera, M]] | ||
[[Category: Heme binding protein]] | [[Category: Heme binding protein]] | ||
[[Category: Transport protein]] | [[Category: Transport protein]] | ||
Revision as of 15:13, 21 December 2014
2.2A resolution structure of Holo hemophore HasA from Yersinia pestis2.2A resolution structure of Holo hemophore HasA from Yersinia pestis
Structural highlights
Publication Abstract from PubMedHemophores from Serratia marcescens (HasAsm) and Pseudomonas aeruginosa (HasAp) bind hemin between two loops, which harbor the axial ligands H32 and Y75. Hemin binding to the Y75 loop triggers closing of the H32 loop and enables binding of H32. Because Yersinia pestis HasA (HasAyp) presents a Gln at position 32, we determined the structures of apo- and holo-HasAyp. Surprisingly, the Q32 loop in apo-HasAyp is already in the closed conformation, but no residue from the Q32 loop binds hemin in holo-HasAyp. In agreement with the minimal reorganization between the apo- and holo-structures, the hemin on-rate is too fast to detect by conventional stopped-flow measurements. The Hemophore HasA from Yersinia pestis (HasAyp) Coordinates Hemin with a Single Residue, Tyr75, and with Minimal Conformational Change.,Kumar R, Lovell S, Matsumura H, Battaile KP, Moenne-Loccoz P, Rivera M Biochemistry. 2013 Apr 23;52(16):2705-7. doi: 10.1021/bi400280z. Epub 2013 Apr, 11. PMID:23578210[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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