4jes: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==1.6A resolution Apo structure of the hemophore HasA from Yersinia pestis (Hexagonal Form)== | ==1.6A resolution Apo structure of the hemophore HasA from Yersinia pestis (Hexagonal Form)== | ||
<StructureSection load='4jes' size='340' side='right' caption='[[4jes]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='4jes' size='340' side='right'caption='[[4jes]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4jes]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4jes]] is a 2 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=4JES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4JES FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</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=4jes FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jes OCA], [https://pdbe.org/4jes PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4jes RCSB], [https://www.ebi.ac.uk/pdbsum/4jes PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4jes ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q0WA92_YERPE Q0WA92_YERPE] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 22: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Yersinia pestis]] | ||
[[Category: | [[Category: Battaile KP]] | ||
[[Category: | [[Category: Kumar R]] | ||
[[Category: | [[Category: Lovell S]] | ||
[[Category: | [[Category: Rivera M]] | ||
Revision as of 14:09, 24 November 2022
1.6A resolution Apo structure of the hemophore HasA from Yersinia pestis (Hexagonal Form)1.6A resolution Apo structure of the hemophore HasA from Yersinia pestis (Hexagonal Form)
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
|
| ||||||||||||||||