6zqq: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Structure of the Pmt3-MIR domain with bound ligands== | ==Structure of the Pmt3-MIR domain with bound ligands== | ||
<StructureSection load='6zqq' size='340' side='right'caption='[[6zqq]]' scene=''> | <StructureSection load='6zqq' size='340' side='right'caption='[[6zqq]], [[Resolution|resolution]] 1.90Å' 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=6ZQQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ZQQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[6zqq]] is a 4 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=6ZQQ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6ZQQ 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=6zqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zqq OCA], [http://pdbe.org/6zqq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zqq RCSB], [http://www.ebi.ac.uk/pdbsum/6zqq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zqq 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></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PMT3, GI526_G0005657 ([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=6zqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zqq OCA], [http://pdbe.org/6zqq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6zqq RCSB], [http://www.ebi.ac.uk/pdbsum/6zqq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6zqq ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/A0A6A5Q4I2_YEASX A0A6A5Q4I2_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 6zqq" 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 Pmt3-MIR domain with bound ligands
| ||||||||||||
