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== | ==2.2A resolution structure of Holo hemophore HasA from Yersinia pestis== | ||
[[4jet]] is a 10 chain structure with sequence from [ | <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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4JET FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=4jet FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jet OCA], [https://pdbe.org/4jet PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jet RCSB], [https://www.ebi.ac.uk/pdbsum/4jet PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jet ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q0WA92_YERPE Q0WA92_YERPE] | |||
<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> | |||
<ref | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4jet" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Yersinia pestis]] | [[Category: Yersinia pestis]] | ||
[[Category: Battaile | [[Category: Battaile KP]] | ||
[[Category: Kumar | [[Category: Kumar R]] | ||
[[Category: Lovell | [[Category: Lovell S]] | ||
[[Category: Rivera | [[Category: Rivera M]] | ||
Latest revision as of 18:41, 20 September 2023
2.2A resolution structure of Holo hemophore HasA from Yersinia pestis2.2A resolution structure of Holo hemophore HasA from Yersinia pestis
Structural highlights
FunctionPublication 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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