4pq1: Difference between revisions
New page: '''Unreleased structure''' The entry 4pq1 is ON HOLD Authors: Um, S.H., Kim, J.S., Yoon, B.Y., Ha, N.C. Description: Crystal structure and functional implications of a DsbF homologue f... |
No edit summary |
||
| (8 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==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=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4pq1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_diphtheriae_NCTC_13129 Corynebacterium diphtheriae NCTC 13129]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4PQ1 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]] 2.097Å</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=4pq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pq1 OCA], [https://pdbe.org/4pq1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pq1 RCSB], [https://www.ebi.ac.uk/pdbsum/4pq1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pq1 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6NJJ0_CORDI Q6NJJ0_CORDI] | |||
<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__ | |||
</StructureSection> | |||
[[Category: Corynebacterium diphtheriae NCTC 13129]] | |||
[[Category: Large Structures]] | |||
[[Category: Ha NC]] | |||
[[Category: Kim JS]] | |||
[[Category: Um SH]] | |||
[[Category: Yoon BY]] | |||
Latest revision as of 11:29, 9 October 2024
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
FunctionPublication 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
|
| ||||||||||||||||