3boa
From Proteopedia
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- | [[Image:3boa.png|left|200px]] | ||
- | + | ==Crystal structure of yeast protein disulfide isomerase.== | |
+ | <StructureSection load='3boa' size='340' side='right'caption='[[3boa]], [[Resolution|resolution]] 3.70Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3boa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_W303 Saccharomyces cerevisiae W303]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BOA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BOA FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.7Å</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=3boa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3boa OCA], [https://pdbe.org/3boa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3boa RCSB], [https://www.ebi.ac.uk/pdbsum/3boa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3boa ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/PDI_YEAST PDI_YEAST] Protein disulfide isomerase of ER lumen required for formation of disulfide bonds in secretory and cell-surface proteins and which unscrambles non-native disulfide bonds. Forms a complex with MNL1 to process unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2, promoting degradation in unfolded protein response.<ref>PMID:16002399</ref> <ref>PMID:19124653</ref> <ref>PMID:21700223</ref> | ||
+ | == 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/bo/3boa_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=3boa ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Protein-disulfide isomerase (PDI) catalyzes the formation of the correct pattern of disulfide bonds in secretory proteins. A low resolution crystal structure of yeast PDI described here reveals large scale conformational changes compared with the initially reported structure, indicating that PDI is a highly flexible molecule with its catalytic domains, a and a', representing two mobile arms connected to a more rigid core composed of the b and b' domains. Limited proteolysis revealed that the linker between the a domain and the core is more susceptible to degradation than that connecting the a' domain to the core. By restricting the two arms with inter-domain disulfide bonds, the molecular flexibility of PDI, especially that of its a domain, was demonstrated to be essential for the enzymatic activity in vitro and in vivo. The crystal structure also featured a PDI dimer, and a propensity to dimerize in solution and in the ER was confirmed by cross-linking experiments and the split green fluorescent protein system. Although sedimentation studies suggested that the self-association of PDI is weak, we hypothesize that PDI exists as an interconvertible mixture of monomers and dimers in the endoplasmic reticulum due to its high abundance in this compartment. | ||
- | + | The catalytic activity of protein-disulfide isomerase requires a conformationally flexible molecule.,Tian G, Kober FX, Lewandrowski U, Sickmann A, Lennarz WJ, Schindelin H J Biol Chem. 2008 Nov 28;283(48):33630-40. Epub 2008 Sep 24. PMID:18815132<ref>PMID:18815132</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 3boa" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | == | + | __TOC__ |
- | < | + | </StructureSection> |
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: Saccharomyces cerevisiae]] | + | [[Category: Saccharomyces cerevisiae W303]] |
- | [[Category: Lennarz | + | [[Category: Lennarz WJ]] |
- | [[Category: Schindelin | + | [[Category: Schindelin H]] |
- | [[Category: Tian | + | [[Category: Tian G]] |
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Current revision
Crystal structure of yeast protein disulfide isomerase.
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