2k8v: Difference between revisions
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==Solution structure of Oxidised ERp18== | ==Solution structure of Oxidised ERp18== | ||
<StructureSection load='2k8v' size='340' side='right'caption='[[2k8v | <StructureSection load='2k8v' size='340' side='right'caption='[[2k8v]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2k8v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2k8v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K8V 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">Solution NMR, 40 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=2k8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k8v OCA], [https://pdbe.org/2k8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k8v RCSB], [https://www.ebi.ac.uk/pdbsum/2k8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k8v 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=2k8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k8v OCA], [https://pdbe.org/2k8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k8v RCSB], [https://www.ebi.ac.uk/pdbsum/2k8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k8v ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/TXD12_HUMAN TXD12_HUMAN] Possesses significant protein thiol-disulfide oxidase activity.<ref>PMID:12761212</ref> | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k8/2k8v_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k8/2k8v_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
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</div> | </div> | ||
<div class="pdbe-citations 2k8v" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2k8v" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[ER-resident protein|ER-resident protein]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Alanen | [[Category: Alanen HI]] | ||
[[Category: Howard | [[Category: Howard MJ]] | ||
[[Category: Kelly | [[Category: Kelly G]] | ||
[[Category: Rowe | [[Category: Rowe ML]] | ||
[[Category: Ruddock | [[Category: Ruddock LW]] | ||
[[Category: Schmidt | [[Category: Schmidt JM]] | ||
[[Category: Williamson | [[Category: Williamson RA]] | ||
Latest revision as of 10:41, 9 October 2024
Solution structure of Oxidised ERp18Solution structure of Oxidised ERp18
Structural highlights
FunctionTXD12_HUMAN Possesses significant protein thiol-disulfide oxidase activity.[1] 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 PubMedHere we report the solution structure of oxidized ERp18 as determined using NMR spectroscopy. ERp18 is the smallest member of the protein disulfide isomerase (PDI) family of proteins to contain a Cys-Xxx-Xxx-Cys active site motif. It is an 18 kDa endoplasmic reticulum resident protein with unknown function although sequence similarity to individual domains of the thiol-disulfide oxidoreductase PDI suggests ERp18 may have a similar structure and function. Like the catalytic domains of PDI, ERp18 adopts a thioredoxin fold with a thioredoxin-like active site located at the N-terminus of a long kinked helix that spans the length of the protein. Comparison of backbone chemical shifts for oxidized and reduced ERp18 shows the majority of residues possess the same backbone conformation in both states, with differences limited to the active site and regions in close proximity. S(2) order parameters from NMR backbone dynamics were found to be 0.81 for oxidized and 0.91 for reduced ERp18, and these observations, in combination with amide hydrogen exchange rates, imply a more rigid and compact backbone for the reduced structure. These observations support a putative role for ERp18 within the cell as an oxidase, introducing disulfide bonds to substrate proteins, providing structural confirmation of ERp18's role as a thiol-disulfide oxidoreductase. Solution Structure and Dynamics of ERp18, a Small Endoplasmic Reticulum Resident Oxidoreductase .,Rowe ML, Ruddock LW, Kelly G, Schmidt JM, Williamson RA, Howard MJ Biochemistry. 2009 May 7. PMID:19361226[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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