6p25: Difference between revisions

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<SX load='6p25' size='340' side='right' viewer='molstar' caption='[[6p25]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<SX load='6p25' size='340' side='right' viewer='molstar' caption='[[6p25]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6p25]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_w303 Saccharomyces cerevisiae w303]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P25 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6P25 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6p25]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_W303 Saccharomyces cerevisiae W303]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P25 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CPL:1-PALMITOYL-2-LINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>CPL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NNM:(3R)-3,31-dimethyl-7,11,15,19,23,27-hexamethylidenedotriacont-31-en-1-yl+dihydrogen+phosphate'>NNM</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PMT1, YDL095W, D2390 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=580240 Saccharomyces cerevisiae W303]), PMT2, FUN25, YAL023C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=580240 Saccharomyces cerevisiae W303])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CPL:1-PALMITOYL-2-LINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>CPL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NNM:[(3~{R})-3,31-dimethyl-7,11,15,19,23,27-hexamethylidene-dotriacont-31-enyl]+dihydrogen+phosphate'>NNM</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dolichyl-phosphate-mannose--protein_mannosyltransferase Dolichyl-phosphate-mannose--protein mannosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.109 2.4.1.109] </span></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=6p25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p25 OCA], [https://pdbe.org/6p25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p25 RCSB], [https://www.ebi.ac.uk/pdbsum/6p25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p25 ProSAT]</span></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=6p25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p25 OCA], [http://pdbe.org/6p25 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6p25 RCSB], [http://www.ebi.ac.uk/pdbsum/6p25 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6p25 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PMT1_YEAST PMT1_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 PMT3 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. Required for incorporation of proteins in the cell wall.<ref>PMID:10764776</ref> <ref>PMID:18182384</ref> <ref>PMID:8367478</ref> <ref>PMID:8543034</ref> <ref>PMID:9466258</ref> [[http://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> 
[https://www.uniprot.org/uniprot/PMT1_YEAST PMT1_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 PMT3 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. Required for incorporation of proteins in the cell wall.<ref>PMID:10764776</ref> <ref>PMID:18182384</ref> <ref>PMID:8367478</ref> <ref>PMID:8543034</ref> <ref>PMID:9466258</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</SX>
</SX>
[[Category: Dolichyl-phosphate-mannose--protein mannosyltransferase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae w303]]
[[Category: Saccharomyces cerevisiae W303]]
[[Category: Bai, L]]
[[Category: Bai L]]
[[Category: Li, H]]
[[Category: Li H]]
[[Category: Complex]]
[[Category: Glycosylation]]
[[Category: Transferase]]
Retrieved from "https://proteopedia.org/6p25"