4pq1: Difference between revisions
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==Crystal structure and functional implications of a DsbF homologue from Corynebacterium diphtheriae== | ==Crystal structure and functional implications of a DsbF homologue from Corynebacterium diphtheriae== | ||
<StructureSection load='4pq1' size='340' side='right' caption='[[4pq1]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='4pq1' size='340' side='right'caption='[[4pq1]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4pq1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cordi Cordi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PQ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PQ1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4pq1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cordi Cordi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PQ1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PQ1 FirstGlance]. <br> | ||
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<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=4pq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pq1 OCA], [http://pdbe.org/4pq1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pq1 RCSB], [http://www.ebi.ac.uk/pdbsum/4pq1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pq1 ProSAT]</span></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=4pq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pq1 OCA], [http://pdbe.org/4pq1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4pq1 RCSB], [http://www.ebi.ac.uk/pdbsum/4pq1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4pq1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Disulfide-bond formation, mediated by the Dsb family of proteins, is important in the correct folding of secreted or extracellular proteins in bacteria. In Gram-negative bacteria, disulfide bonds are introduced into the folding proteins in the periplasm by DsbA. DsbE from Escherichia coli has been implicated in the reduction of disulfide bonds in the maturation of cytochrome c. The Gram-positive bacterium Mycobacterium tuberculosis encodes DsbE and its homologue DsbF, the structures of which have been determined. However, the two mycobacterial proteins are able to oxidatively fold a protein in vitro, unlike DsbE from E. coli. In this study, the crystal structure of a DsbE or DsbF homologue protein from Corynebacterium diphtheriae has been determined, which revealed a thioredoxin-like domain with a typical CXXC active site. Structural comparison with M. tuberculosis DsbF would help in understanding the function of the C. diphtheriae protein. | |||
Structure of a DsbF homologue from Corynebacterium diphtheriae.,Um SH, Kim JS, Lee K, Ha NC Acta Crystallogr F Struct Biol Commun. 2014 Sep;70(Pt 9):1167-72. doi:, 10.1107/S2053230X14016355. Epub 2014 Aug 29. PMID:25195886<ref>PMID:25195886</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4pq1" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Cordi]] | [[Category: Cordi]] | ||
[[Category: Large Structures]] | |||
[[Category: Ha, N C]] | [[Category: Ha, N C]] | ||
[[Category: Kim, J S]] | [[Category: Kim, J S]] | ||
Revision as of 11:41, 1 January 2020
Crystal structure and functional implications of a DsbF homologue from Corynebacterium diphtheriaeCrystal structure and functional implications of a DsbF homologue from Corynebacterium diphtheriae
Structural highlights
Publication Abstract from PubMedDisulfide-bond formation, mediated by the Dsb family of proteins, is important in the correct folding of secreted or extracellular proteins in bacteria. In Gram-negative bacteria, disulfide bonds are introduced into the folding proteins in the periplasm by DsbA. DsbE from Escherichia coli has been implicated in the reduction of disulfide bonds in the maturation of cytochrome c. The Gram-positive bacterium Mycobacterium tuberculosis encodes DsbE and its homologue DsbF, the structures of which have been determined. However, the two mycobacterial proteins are able to oxidatively fold a protein in vitro, unlike DsbE from E. coli. In this study, the crystal structure of a DsbE or DsbF homologue protein from Corynebacterium diphtheriae has been determined, which revealed a thioredoxin-like domain with a typical CXXC active site. Structural comparison with M. tuberculosis DsbF would help in understanding the function of the C. diphtheriae protein. Structure of a DsbF homologue from Corynebacterium diphtheriae.,Um SH, Kim JS, Lee K, Ha NC Acta Crystallogr F Struct Biol Commun. 2014 Sep;70(Pt 9):1167-72. doi:, 10.1107/S2053230X14016355. Epub 2014 Aug 29. PMID:25195886[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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