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3boa

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{{Seed}}
 
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[[Image:3boa.png|left|200px]]
 
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==Crystal structure of yeast protein disulfide isomerase.==
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The line below this paragraph, containing "STRUCTURE_3boa", creates the "Structure Box" on the page.
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<StructureSection load='3boa' size='340' side='right'caption='[[3boa]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.7&#8491;</td></tr>
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<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>
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{{STRUCTURE_3boa| PDB=3boa | SCENE= }}
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bo/3boa_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===Crystal structure of yeast protein disulfide isomerase.===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_18815132}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3boa" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18815132 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18815132}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3BOA is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BOA OCA].
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[[Category: Saccharomyces cerevisiae W303]]
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[[Category: Lennarz WJ]]
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==Reference==
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[[Category: Schindelin H]]
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<ref group="xtra">PMID:18815132</ref><references group="xtra"/>
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[[Category: Tian G]]
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[[Category: Protein disulfide-isomerase]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Lennarz, W J.]]
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[[Category: Schindelin, H.]]
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[[Category: Tian, G.]]
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[[Category: Disulfide bond formation]]
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[[Category: Endoplasmic reticulum]]
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[[Category: Glycoprotein]]
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[[Category: Isomerase]]
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[[Category: Molecular flexibility]]
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[[Category: Protein folding]]
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[[Category: Redox-active center]]
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[[Category: Thioredoxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 19:50:55 2009''
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Current revision

Crystal structure of yeast protein disulfide isomerase.

PDB ID 3boa

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