5hfg: Difference between revisions
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==Cytosolic disulfide reductase DsbM from Pseudomonas aeruginosa== | ==Cytosolic disulfide reductase DsbM from Pseudomonas aeruginosa== | ||
<StructureSection load='5hfg' size='340' side='right' caption='[[5hfg]], [[Resolution|resolution]] 1.82Å' scene=''> | <StructureSection load='5hfg' size='340' side='right'caption='[[5hfg]], [[Resolution|resolution]] 1.82Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5hfg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HFG OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5hfg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HFG FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.823Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5hfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hfg OCA], [https://pdbe.org/5hfg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hfg RCSB], [https://www.ebi.ac.uk/pdbsum/5hfg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hfg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9I774_PSEAE Q9I774_PSEAE] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 16: | Line 18: | ||
</div> | </div> | ||
<div class="pdbe-citations 5hfg" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5hfg" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pseudomonas aeruginosa PAO1]] | ||
[[Category: | [[Category: Ha N-C]] | ||
[[Category: | [[Category: Jo I]] | ||
Latest revision as of 10:34, 9 August 2023
Cytosolic disulfide reductase DsbM from Pseudomonas aeruginosaCytosolic disulfide reductase DsbM from Pseudomonas aeruginosa
Structural highlights
FunctionPublication Abstract from PubMedIn bacteria, many Dsb-family proteins play diverse roles in the conversion between the oxidized and reduced states of cysteine residues of substrate proteins. Most Dsb enzymes catalyze disulfide formation in periplasmic or secreted substrate proteins. Recently, a DsbM protein has been found in a Gram-negative bacterium, and was characterized as a cytosolic Dsb member with the conserved CXXC motif on the basis of sequence homology to the Dsb-family proteins. The protein was implicated in the reduction of the cytoplasmic redox-sensor protein OxyR in Pseudomonas aeruginosa. Here, crystal structures of DsbM from P. aeruginosa are presented, revealing that it consists of a modified thioredoxin domain containing the CXXC motif and a lid domain surrounding the CXXC motif. In a glutathione-linked structure, a glutathione molecule is linked to the CXXC motif of DsbM and is bound in an elongated cavity region in the thioredoxin domain, which is also suited for substrate peptide binding. A striking structural similarity to a human glutathione S-transferase was found in the glutathione-binding pocket. Further, biochemical evidence is presented suggesting that DsbM is directly involved in the reduction of the disulfide of Cys199 and Cys208 in OxyR, resulting in the acceleration of OxyR reduction in the absence of reactive oxygen species stress. These findings may help to expand the understanding of the diverse roles of redox-related proteins that contain the CXXC motif. Crystal structures of the disulfide reductase DsbM from Pseudomonas aeruginosa.,Jo I, Park N, Chung IY, Cho YH, Ha NC Acta Crystallogr D Struct Biol. 2016 Oct 1;72(Pt 10):1100-1109. Epub 2016 Sep 15. PMID:27710931[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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