View source for 4fyb


==Structural and functional characterizations of a thioredoxin-fold protein from Helicobacter pylori==
<StructureSection load='4fyb' size='340' side='right'caption='[[4fyb]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O25140_HELPY O25140_HELPY] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Maturation 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<ref>PMID:23633582</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</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/>
__TOC__
</StructureSection>
[[Category: Helicobacter pylori 26695]]
[[Category: Large Structures]]
[[Category: An DR]]
[[Category: Han BW]]
[[Category: Im HN]]
[[Category: Kim HS]]
[[Category: Kim J]]
[[Category: Kim JY]]
[[Category: Kim S]]
[[Category: Lee SJ]]
[[Category: Suh SW]]
[[Category: Yoon H]]
[[Category: Yoon JY]]