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9i5k
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the Chaetomium thermophilum Pmt4 homodimer (C2 symmetry)== | |
| + | <StructureSection load='9i5k' size='340' side='right'caption='[[9i5k]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9i5k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum Chaetomium thermophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9I5K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9I5K FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1I0M:[(3~{S},6~{E},10~{Z},14~{Z},18~{Z},22~{Z},26~{Z},30~{Z})-3,7,11,15,19,23,27,31-octamethyltritriaconta-6,10,14,18,22,26,30-heptaenyl]+dihydrogen+phosphate'>A1I0M</scene>, <scene name='pdbligand=A1I0N:[(3~{S},6~{E},10~{Z},14~{Z},18~{Z},22~{Z})-3,7,11,15,19,23-hexamethylpentacosa-6,10,14,18,22-pentaenyl]+[(2~{S},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]+hydrogen+phosphate'>A1I0N</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=9i5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9i5k OCA], [https://pdbe.org/9i5k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9i5k RCSB], [https://www.ebi.ac.uk/pdbsum/9i5k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9i5k ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/G0SET1_CHATD G0SET1_CHATD] 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) are conserved endoplasmic reticulum membrane-embedded enzymes responsible for the transfer of mannose from dolichol phosphate-mannose (Dol-P-Man) to serine/threonine-rich protein substrates or unfolded proteins. PMTs from three subfamilies form obligate dimers with different substrate specificities and require the concerted action of their transmembrane domains (TMDs) and a luminal MIR domain for catalysis. Here, we present structures, native mass spectrometry, and structure-based mutagenesis of the fungal Pmt4 homodimer. The core fold of the TMDs and MIR domain is conserved with the Pmt1-Pmt2 heterodimer, indicating a shared catalytic mechanism. Distinct from Pmt4, the MIR domain interacts in cis with the TMDs of the same subunit and has a beta-hairpin insertion required for O-mannosylation of substrates. We further identify a cytosolic binding site for substrate Dol-P-Man within the Pmt4 TMDs, which is conserved amongst PMTs and important for in vivo activity. Thus, we provide a framework to understand the substrate specificity and regulation of the Pmt4 homodimer. | ||
| - | + | Structural characterisation of the fungal Pmt4 homodimer.,McDowell MA, Wild K, Fiorentino F, Bausewein D, Metschies A, Chiapparino A, Hackmann Y, Bilsing FL, Brenske D, Mortensen S, Wu D, Robinson CV, Strahl S, Sinning I Nat Commun. 2025 Dec 14;16(1):11134. doi: 10.1038/s41467-025-67412-1. PMID:41392315<ref>PMID:41392315</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9i5k" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Chaetomium thermophilum]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: McDowell MA]] | ||
| + | [[Category: Sinning I]] | ||
| + | [[Category: Wild K]] | ||
Current revision
Structure of the Chaetomium thermophilum Pmt4 homodimer (C2 symmetry)
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