4fyb: Difference between revisions
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== Structural highlights == | == 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> | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </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='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'>[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> | </table> | ||
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
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