3uem

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{{STRUCTURE_3uem| PDB=3uem | SCENE= }}
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==Crystal structure of human PDI bb'a' domains==
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===Crystal structure of human PDI bb'a' domains===
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<StructureSection load='3uem' size='340' side='right' caption='[[3uem]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
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{{ABSTRACT_PUBMED_22090031}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3uem]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UEM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UEM FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=D1D:(4S,5S)-1,2-DITHIANE-4,5-DIOL'>D1D</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<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=3uem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uem OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uem RCSB], [http://www.ebi.ac.uk/pdbsum/3uem PDBsum]</span></td></tr>
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</table>
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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), with domains arranged as abb'xa'c, is a key enzyme and chaperone localized in the endoplasmic reticulum (ER) catalyzing oxidative folding and preventing misfolding/aggregation of proteins. It has been controversial whether the chaperone activity of PDI is redox-regulated, and the molecular basis is unclear. Here, we show that both the chaperone activity and the overall conformation of human PDI are redox-regulated. We further demonstrate that the conformational changes are triggered by the active site of domain a', and the minimum redox-regulated cassette is located in b'xa'. The structure of the reduced bb'xa' reveals for the first time that domain a' packs tightly with both domain b' and linker x to form one compact structural module. Oxidation of domain a' releases the compact conformation and exposes the shielded hydrophobic areas to facilitate its high chaperone activity. Thus, the study unequivocally provides mechanistic insights into the redox-regulated chaperone activity of human PDI.
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==Function==
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Human protein-disulfide isomerase is a redox-regulated chaperone activated by oxidation of domain a'.,Wang C, Yu J, Huo L, Wang L, Feng W, Wang CC J Biol Chem. 2012 Jan 6;287(2):1139-49. Epub 2011 Nov 16. PMID:22090031<ref>PMID:22090031</ref>
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[[http://www.uniprot.org/uniprot/PDIA1_HUMAN PDIA1_HUMAN]] This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP.<ref>PMID:10636893</ref> <ref>PMID:12485997</ref>
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[3uem]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UEM OCA].
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</div>
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:022090031</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein disulfide-isomerase]]
[[Category: Protein disulfide-isomerase]]
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[[Category: Feng, W.]]
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[[Category: Feng, W]]
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[[Category: Huo, L.]]
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[[Category: Huo, L]]
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[[Category: Wang, C.]]
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[[Category: Wang, C]]
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[[Category: Wang, C C.]]
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[[Category: Wang, C C]]
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[[Category: Yu, J.]]
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[[Category: Yu, J]]
[[Category: Chaperone]]
[[Category: Chaperone]]
[[Category: Protein disulfide isomerase]]
[[Category: Protein disulfide isomerase]]
[[Category: Thioredoxin-like domain]]
[[Category: Thioredoxin-like domain]]

Revision as of 06:37, 21 December 2014

Crystal structure of human PDI bb'a' domains

3uem, resolution 2.29Å

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