2ruf
From Proteopedia
(Difference between revisions)
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<StructureSection load='2ruf' size='340' side='right'caption='[[2ruf]]' scene=''> | <StructureSection load='2ruf' size='340' side='right'caption='[[2ruf]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full | + | <table><tr><td colspan='2'>[[2ruf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Humicola_insolens Humicola insolens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RUF FirstGlance]. <br> |
</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=2ruf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ruf OCA], [https://pdbe.org/2ruf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ruf RCSB], [https://www.ebi.ac.uk/pdbsum/2ruf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ruf ProSAT]</span></td></tr> | </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=2ruf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ruf OCA], [https://pdbe.org/2ruf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ruf RCSB], [https://www.ebi.ac.uk/pdbsum/2ruf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ruf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PDI_HUMIN PDI_HUMIN] Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Protein disulfide isomerase functions as a folding catalyst in the endoplasmic reticulum. Its b' and a' domains provide substrate-binding sites and undergo a redox-dependent domain rearrangement coupled to an open-closed structural change. Here we determined the first solution structure of the a' domain in its oxidized form and thereby demonstrate that oxidation of the a' domain induces significant conformational changes not only in the vicinity of the active site but also in the distal b'-interfacial segment. Based on these findings, we propose that this conformational transition triggers the domain segregation coupled with the exposure of the hydrophobic surface. | ||
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| + | Redox-coupled structural changes of the catalytic a' domain of protein disulfide isomerase.,Inagaki K, Satoh T, Yagi-Utsumi M, Le Gulluche AC, Anzai T, Uekusa Y, Kamiya Y, Kato K FEBS Lett. 2015 Aug 10. pii: S0014-5793(15)00689-4. doi:, 10.1016/j.febslet.2015.07.041. PMID:26272828<ref>PMID:26272828</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 2ruf" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Humicola insolens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Inagaki K]] | [[Category: Inagaki K]] | ||
[[Category: Kato K]] | [[Category: Kato K]] | ||
[[Category: Satoh T]] | [[Category: Satoh T]] | ||
Current revision
Solution structure of the a' domain of thermophilic fungal protein disulfide (reduced form, 303K)
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