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| | ==Solution structure of the a' domain of thermophilic fungal protein disulfide (reduced form, 303K)== | | ==Solution structure of the a' domain of thermophilic fungal protein disulfide (reduced form, 303K)== |
| - | <StructureSection load='2ruf' size='340' side='right' caption='[[2ruf]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2ruf' size='340' side='right'caption='[[2ruf]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ruf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_16454 Atcc 16454]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RUF FirstGlance]. <br> | + | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2kp1|2kp1]], [[2kp2|2kp2]]</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> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] </span></td></tr>
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| - | <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=2ruf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ruf OCA], [http://pdbe.org/2ruf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ruf RCSB], [http://www.ebi.ac.uk/pdbsum/2ruf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ruf ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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). | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 16454]] | + | [[Category: Humicola insolens]] |
| - | [[Category: Protein disulfide-isomerase]] | + | [[Category: Large Structures]] |
| - | [[Category: Inagaki, K]] | + | [[Category: Inagaki K]] |
| - | [[Category: Kato, K]] | + | [[Category: Kato K]] |
| - | [[Category: Satoh, T]] | + | [[Category: Satoh T]] |
| - | [[Category: Disulfide bond]]
| + | |
| - | [[Category: Endoplasmic reticulum]]
| + | |
| - | [[Category: Isomerase]]
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| - | [[Category: Redox-active center]]
| + | |
| - | [[Category: Thioredoxin fold]]
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| Structural highlights
Function
PDI_HUMIN Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer (By similarity).
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Inagaki K, Satoh T, Yagi-Utsumi M, Le Gulluche AC, Anzai T, Uekusa Y, Kamiya Y, Kato K. Redox-coupled structural changes of the catalytic a' domain of protein disulfide isomerase. FEBS Lett. 2015 Aug 10. pii: S0014-5793(15)00689-4. doi:, 10.1016/j.febslet.2015.07.041. PMID:26272828 doi:http://dx.doi.org/10.1016/j.febslet.2015.07.041
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