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6zqp
From Proteopedia
(Difference between revisions)
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==Structure of the Pmt2-MIR domain with bound ligands== | ==Structure of the Pmt2-MIR domain with bound ligands== | ||
| - | <StructureSection load='6zqp' size='340' side='right'caption='[[6zqp]]' scene=''> | + | <StructureSection load='6zqp' size='340' side='right'caption='[[6zqp]], [[Resolution|resolution]] 1.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>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 [http://proteopedia.org/fgij/fg.htm?mol=6ZQP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6zqp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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 [http://proteopedia.org/fgij/fg.htm?mol=6ZQP FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6zqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zqp OCA], [http://pdbe.org/6zqp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zqp RCSB], [http://www.ebi.ac.uk/pdbsum/6zqp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zqp ProSAT]</span></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PMT2, GI526_G0000041 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6zqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zqp OCA], [http://pdbe.org/6zqp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zqp RCSB], [http://www.ebi.ac.uk/pdbsum/6zqp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zqp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/A0A6A5PTF1_YEASX A0A6A5PTF1_YEASX]] Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.[RuleBase:RU367007] | ||
| + | <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> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6zqp" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 18824]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Chiapparino A]] | + | [[Category: Chiapparino, A]] |
| - | [[Category: Hackmann Y]] | + | [[Category: Hackmann, Y]] |
| - | [[Category: Mortensen S]] | + | [[Category: Mortensen, S]] |
| - | [[Category: Sinning I]] | + | [[Category: Sinning, I]] |
| - | [[Category: Wild K]] | + | [[Category: Wild, K]] |
| + | [[Category: Beta-trefoil]] | ||
| + | [[Category: Carbohydrate-binding module]] | ||
| + | [[Category: Mir domain]] | ||
| + | [[Category: Peptide binding protein]] | ||
| + | [[Category: Protein-o-mannosylation]] | ||
Revision as of 06:03, 20 January 2021
Structure of the Pmt2-MIR domain with bound ligands
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