2ju5: Difference between revisions
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==DsbH Oxidoreductase== | |||
<StructureSection load='2ju5' size='340' side='right'caption='[[2ju5]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2ju5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydia_pneumoniae_TW-183 Chlamydia pneumoniae TW-183]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JU5 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2ju5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ju5 OCA], [https://pdbe.org/2ju5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ju5 RCSB], [https://www.ebi.ac.uk/pdbsum/2ju5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ju5 ProSAT]</span></td></tr> | |||
</table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ju/2ju5_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ju5 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Chlamydia family of human pathogens uses outer envelope proteins that are highly cross-linked by disulfide bonds but nevertheless keeps an unusually high number of unpaired cysteines in its secreted proteins. To gain insight into chlamydial disulfide bond catalysis, the structure, function, and substrate interaction of a novel periplasmic oxidoreductase, termed DsbH, were determined. The structure of DsbH, its redox potential of -269 mV, and its functional properties are similar to thioredoxin and the C-terminal domain of DsbD, i.e. characteristic of a disulfide reductase. As compared with these proteins, the two central residues of the DsbH catalytic motif (CMWC) shield the catalytic disulfide bond and are selectively perturbed by a peptide ligand. This shows that these oxidoreductase family characteristic residues are not only important in determining the redox potential of the catalytic disulfide bond but also in influencing substrate interactions. For DsbH, three functional roles are conceivable; that is, reducing intermolecular disulfides between proteins and small molecules, keeping a specific subset of exported proteins reduced, or maintaining the periplasm of Chlamydia in a generally reducing state. | |||
Insight into disulfide bond catalysis in Chlamydia from the structure and function of DsbH, a novel oxidoreductase.,Mac TT, von Hacht A, Hung KC, Dutton RJ, Boyd D, Bardwell JC, Ulmer TS J Biol Chem. 2008 Jan 11;283(2):824-32. Epub 2007 Nov 14. PMID:18003611<ref>PMID:18003611</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2ju5" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Thiol:disulfide interchange protein 3D structures|Thiol:disulfide interchange protein 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
[[Category: Chlamydia pneumoniae]] | </StructureSection> | ||
[[Category: | [[Category: Chlamydia pneumoniae TW-183]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Ulmer TS]] | |||
Latest revision as of 09:08, 27 November 2024
DsbH OxidoreductaseDsbH Oxidoreductase
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe Chlamydia family of human pathogens uses outer envelope proteins that are highly cross-linked by disulfide bonds but nevertheless keeps an unusually high number of unpaired cysteines in its secreted proteins. To gain insight into chlamydial disulfide bond catalysis, the structure, function, and substrate interaction of a novel periplasmic oxidoreductase, termed DsbH, were determined. The structure of DsbH, its redox potential of -269 mV, and its functional properties are similar to thioredoxin and the C-terminal domain of DsbD, i.e. characteristic of a disulfide reductase. As compared with these proteins, the two central residues of the DsbH catalytic motif (CMWC) shield the catalytic disulfide bond and are selectively perturbed by a peptide ligand. This shows that these oxidoreductase family characteristic residues are not only important in determining the redox potential of the catalytic disulfide bond but also in influencing substrate interactions. For DsbH, three functional roles are conceivable; that is, reducing intermolecular disulfides between proteins and small molecules, keeping a specific subset of exported proteins reduced, or maintaining the periplasm of Chlamydia in a generally reducing state. Insight into disulfide bond catalysis in Chlamydia from the structure and function of DsbH, a novel oxidoreductase.,Mac TT, von Hacht A, Hung KC, Dutton RJ, Boyd D, Bardwell JC, Ulmer TS J Biol Chem. 2008 Jan 11;283(2):824-32. Epub 2007 Nov 14. PMID:18003611[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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