8eoj

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'''Unreleased structure'''
 
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The entry 8eoj is ON HOLD until Paper Publication
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==Microsomal triglyceride transfer protein==
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<StructureSection load='8eoj' size='340' side='right'caption='[[8eoj]], [[Resolution|resolution]] 3.07&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8eoj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EOJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EOJ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.07&#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=8eoj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8eoj OCA], [https://pdbe.org/8eoj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8eoj RCSB], [https://www.ebi.ac.uk/pdbsum/8eoj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8eoj ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We applied raw human liver microsome lysate to a holey carbon grid and used cryo-electron microscopy (cryo-EM) to define its composition. From this sample we identified and simultaneously determined high-resolution structural information for ten unique human liver enzymes involved in diverse cellular processes. Notably, we determined the structure of the endoplasmic bifunctional protein H6PD, where the N- and C-terminal domains independently possess glucose-6-phosphate dehydrogenase and 6-phosphogluconolactonase enzymatic activity, respectively. We also obtained the structure of heterodimeric human GANAB, an ER glycoprotein quality-control machinery that contains a catalytic alpha subunit and a noncatalytic beta subunit. In addition, we observed a decameric peroxidase, PRDX4, which directly contacts a disulfide isomerase-related protein, ERp46. Structural data suggest that several glycosylations, bound endogenous compounds, and ions associate with these human liver enzymes. These results highlight the importance of cryo-EM in facilitating the elucidation of human organ proteomics at the atomic level.
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Authors:
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High-resolution structural-omics of human liver enzymes.,Su CC, Lyu M, Zhang Z, Miyagi M, Huang W, Taylor DJ, Yu EW Cell Rep. 2023 Jun 27;42(6):112609. doi: 10.1016/j.celrep.2023.112609. Epub 2023 , Jun 7. PMID:37289586<ref>PMID:37289586</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 8eoj" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Zhang Z]]

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Microsomal triglyceride transfer protein

PDB ID 8eoj

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