4fyb: Difference between revisions
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==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=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4fyb]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FYB FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fyc|4fyc]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HP_0377 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Helicobacter pylori 26695])</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=4fyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fyb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fyb RCSB], [http://www.ebi.ac.uk/pdbsum/4fyb PDBsum]</span></td></tr> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Helicobacter pylori 26695]] | [[Category: Helicobacter pylori 26695]] | ||
[[Category: An, D R | [[Category: An, D R]] | ||
[[Category: Han, B W | [[Category: Han, B W]] | ||
[[Category: Im, H N | [[Category: Im, H N]] | ||
[[Category: Kim, H S | [[Category: Kim, H S]] | ||
[[Category: Kim, J | [[Category: Kim, J]] | ||
[[Category: Kim, J Y | [[Category: Kim, J Y]] | ||
[[Category: Kim, S | [[Category: Kim, S]] | ||
[[Category: Lee, S J | [[Category: Lee, S J]] | ||
[[Category: Suh, S W | [[Category: Suh, S W]] | ||
[[Category: Yoon, H | [[Category: Yoon, H]] | ||
[[Category: Yoon, J Y | [[Category: Yoon, J Y]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Reductase]] | [[Category: Reductase]] | ||
[[Category: Thioredoxin fold]] | [[Category: Thioredoxin fold]] | ||
Revision as of 14:38, 21 December 2014
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
Publication 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. References
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