8kc9

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Current revision (04:51, 18 September 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8kc9 is ON HOLD until 2026-02-06
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==Human collagen prolyl processing enzyme complex, P3H1/CRTAP/PPIB heterotrimer, bound to cyclosporin A==
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<StructureSection load='8kc9' size='340' side='right'caption='[[8kc9]], [[Resolution|resolution]] 3.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8kc9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8KC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8KC9 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]] 3.75&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=BMT:4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE'>BMT</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</scene></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=8kc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8kc9 OCA], [https://pdbe.org/8kc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8kc9 RCSB], [https://www.ebi.ac.uk/pdbsum/8kc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8kc9 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/P3H1_HUMAN P3H1_HUMAN] Osteogenesis imperfecta type 2;Osteogenesis imperfecta type 3. The disease is caused by variants affecting the gene represented in this entry. A splice site mutation leading to the absence of isoform 1 has been reported in 2 OI8 patients. Isoform 1 is the only form predicted to be located in the endoplasmic reticulum, which the appropriate location for the catalysis of collagen hydroxylation. These patients show indeed severely reduced COL1A1 hydroxylation (PubMed:19088120).<ref>PMID:19088120</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/P3H1_HUMAN P3H1_HUMAN] Basement membrane-associated chondroitin sulfate proteoglycan (CSPG). Has prolyl 3-hydroxylase activity catalyzing the post-translational formation of 3-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens, especially types IV and V. May be involved in the secretory pathway of cells. Has growth suppressive activity in fibroblasts.<ref>PMID:10951563</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Collagen posttranslational processing is crucial for its proper assembly and function. Disruption of collagen processing leads to tissue development and structure disorders like osteogenesis imperfecta (OI). OI-related collagen processing machinery includes prolyl 3-hydroxylase 1 (P3H1), peptidyl-prolyl cis-trans isomerase B (PPIB), and cartilage-associated protein (CRTAP), with their structural organization and mechanism unclear. We determine cryo-EM structures of the P3H1/CRTAP/PPIB complex. The active sites of P3H1 and PPIB form a face-to-face bifunctional reaction center, indicating a coupled modification mechanism. The structure of the P3H1/CRTAP/PPIB/collagen peptide complex reveals multiple binding sites, suggesting a substrate interacting zone. Unexpectedly, a dual-ternary complex is observed, and the balance between ternary and dual-ternary states can be altered by mutations in the P3H1/PPIB active site and the addition of PPIB inhibitors. These findings provide insights into the structural basis of collagen processing by P3H1/CRTAP/PPIB and the molecular pathology of collagen-related disorders.
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Authors:
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The structural basis for the collagen processing by human P3H1/CRTAP/PPIB ternary complex.,Li W, Peng J, Yao D, Rao B, Xia Y, Wang Q, Li S, Cao M, Shen Y, Ma P, Liao R, Qin A, Zhao J, Cao Y Nat Commun. 2024 Sep 8;15(1):7844. doi: 10.1038/s41467-024-52321-6. PMID:39245686<ref>PMID:39245686</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 8kc9" 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: Tolypocladium inflatum]]
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[[Category: Cao M]]
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[[Category: Cao Y]]
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[[Category: Li S]]
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[[Category: Li W]]
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[[Category: Liao R]]
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[[Category: Ma P]]
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[[Category: Peng J]]
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[[Category: Qin A]]
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[[Category: Rao B]]
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[[Category: Shen Y]]
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[[Category: Wang Q]]
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[[Category: Xia Y]]
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[[Category: Yao D]]
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[[Category: Zhao J]]

Current revision

Human collagen prolyl processing enzyme complex, P3H1/CRTAP/PPIB heterotrimer, bound to cyclosporin A

PDB ID 8kc9

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