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6zqp
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6zqp is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the Pmt2-MIR domain with bound ligands== | |
| + | <StructureSection load='6zqp' size='340' side='right'caption='[[6zqp]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6zqp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZQP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZQP 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]] 1.6Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6zqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zqp OCA], [https://pdbe.org/6zqp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zqp RCSB], [https://www.ebi.ac.uk/pdbsum/6zqp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zqp ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PMT2_YEAST PMT2_YEAST] Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Forms a heterodimeric complex with PMT2 and more rarely with PMT5 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. The PMT1-PMT2 complex participates in oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export.<ref>PMID:15377669</ref> <ref>PMID:18182384</ref> <ref>PMID:21147851</ref> <ref>PMID:8543034</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Protein O-mannosyltransferases (PMTs) represent a conserved family of multispanning endoplasmic reticulum membrane proteins involved in glycosylation of S/T-rich protein substrates and unfolded proteins. PMTs work as dimers and contain a luminal MIR domain with a beta-trefoil fold, which is susceptive for missense mutations causing alpha-dystroglycanopathies in humans. Here, we analyze PMT-MIR domains by an integrated structural biology approach using X-ray crystallography and NMR spectroscopy and evaluate their role in PMT function in vivo. We determine Pmt2- and Pmt3-MIR domain structures and identify two conserved mannose-binding sites, which are consistent with general beta-trefoil carbohydrate-binding sites (alpha, beta), and also a unique PMT2-subfamily exposed FKR motif. We show that conserved residues in site alpha influence enzyme processivity of the Pmt1-Pmt2 heterodimer in vivo. Integration of the data into the context of a Pmt1-Pmt2 structure and comparison with homologous beta-trefoil - carbohydrate complexes allows for a functional description of MIR domains in protein O-mannosylation. | ||
| - | + | Functional implications of MIR domains in protein O-mannosylation.,Chiapparino A, Grbavac A, Jonker HR, Hackmann Y, Mortensen S, Zatorska E, Schott A, Stier G, Saxena K, Wild K, Schwalbe H, Strahl S, Sinning I Elife. 2020 Dec 24;9. pii: 61189. doi: 10.7554/eLife.61189. PMID:33357379<ref>PMID:33357379</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6zqp" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae]] | ||
| + | [[Category: Chiapparino A]] | ||
| + | [[Category: Hackmann Y]] | ||
| + | [[Category: Mortensen S]] | ||
| + | [[Category: Sinning I]] | ||
| + | [[Category: Wild K]] | ||
Current revision
Structure of the Pmt2-MIR domain with bound ligands
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