4fyb: Difference between revisions
No edit summary |
No edit summary |
||
| (2 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Structural and functional characterizations of a thioredoxin-fold protein from Helicobacter pylori== | ==Structural and functional characterizations of a thioredoxin-fold protein from Helicobacter pylori== | ||
<StructureSection load='4fyb' size='340' side='right' caption='[[4fyb]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='4fyb' size='340' side='right'caption='[[4fyb]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4fyb]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4fyb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FYB 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]] 2.2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4fyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyb OCA], [https://pdbe.org/4fyb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fyb RCSB], [https://www.ebi.ac.uk/pdbsum/4fyb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fyb 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/O25140_HELPY O25140_HELPY] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 16: | Line 18: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4fyb" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 21: | Line 27: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Helicobacter pylori 26695]] | [[Category: Helicobacter pylori 26695]] | ||
[[Category: An | [[Category: Large Structures]] | ||
[[Category: Han | [[Category: An DR]] | ||
[[Category: Im | [[Category: Han BW]] | ||
[[Category: Kim | [[Category: Im HN]] | ||
[[Category: Kim | [[Category: Kim HS]] | ||
[[Category: Kim | [[Category: Kim J]] | ||
[[Category: Kim | [[Category: Kim JY]] | ||
[[Category: Lee | [[Category: Kim S]] | ||
[[Category: Suh | [[Category: Lee SJ]] | ||
[[Category: Yoon | [[Category: Suh SW]] | ||
[[Category: Yoon | [[Category: Yoon H]] | ||
[[Category: Yoon JY]] | |||
Latest revision as of 13:01, 30 October 2024
Structural and functional characterizations of a thioredoxin-fold protein from Helicobacter pyloriStructural and functional characterizations of a thioredoxin-fold protein from Helicobacter pylori
Structural highlights
FunctionPublication Abstract from PubMedMaturation of cytochrome c is carried out in the bacterial periplasm, where specialized thiol-disulfide oxidoreductases provide the correct reduction of oxidized apocytochrome c before covalent haem attachment. HP0377 from Helicobacter pylori is a thioredoxin-fold protein that has been implicated as a component of system II for cytochrome c assembly and shows limited sequence similarity to Escherichia coli DsbC, a disulfide-bond isomerase. To better understand the role of HP0377, its crystal structures have been determined in both reduced and partially oxidized states, which are highly similar to each other. Sedimentation-equilibrium experiments indicate that HP0377 is monomeric in solution. HP0377 adopts a thioredoxin fold but shows distinctive variations as in other thioredoxin-like bacterial periplasmic proteins. The active site of HP0377 closely resembles that of E. coli DsbC. A reductase assay suggests that HP0377 may play a role as a reductase in the biogenesis of holocytochrome c553 (HP1227). Binding experiments indicate that it can form a covalent complex with HP0518, a putative L,D-transpeptidase with a catalytic cysteine residue, via a disulfide bond. Furthermore, physicochemical properties of HP0377 and its R86A variant have been determined. These results suggest that HP0377 may perform multiple functions as a reductase in H. pylori. Structural and functional characterization of HP0377, a thioredoxin-fold protein from Helicobacter pylori.,Yoon JY, Kim J, An DR, Lee SJ, Kim HS, Im HN, Yoon HJ, Kim JY, Kim SJ, Han BW, Suh SW Acta Crystallogr D Biol Crystallogr. 2013 May;69(Pt 5):735-46. doi:, 10.1107/S0907444913001236. Epub 2013 Apr 11. PMID:23633582[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||