4n9w
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4n9w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N9W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N9W FirstGlance]. <br> | <table><tr><td colspan='2'>[[4n9w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N9W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N9W FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.94Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</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=4n9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n9w OCA], [https://pdbe.org/4n9w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n9w RCSB], [https://www.ebi.ac.uk/pdbsum/4n9w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n9w ProSAT]</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=4n9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n9w OCA], [https://pdbe.org/4n9w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n9w RCSB], [https://www.ebi.ac.uk/pdbsum/4n9w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n9w ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/PIMA_MYCS2 PIMA_MYCS2] Catalyzes the addition of a mannose residue from GDP-D-mannose to the position 2 of a phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Contrary to PimB, the mannosyltransferase PimA is unable to transfer a mannose residue to the position 6 of the phosphatidyl-myo-inositola of PIM1.<ref>PMID:12068013</ref> <ref>PMID:19638342</ref> | [https://www.uniprot.org/uniprot/PIMA_MYCS2 PIMA_MYCS2] Catalyzes the addition of a mannose residue from GDP-D-mannose to the position 2 of a phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Contrary to PimB, the mannosyltransferase PimA is unable to transfer a mannose residue to the position 6 of the phosphatidyl-myo-inositola of PIM1.<ref>PMID:12068013</ref> <ref>PMID:19638342</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Secondary structure refolding is a key event in biology as it modulates the conformation of many proteins in the cell, generating functional or aberrant states. The crystal structures of mannosyltransferase PimA reveal an exceptional flexibility of the protein along the catalytic cycle, including beta-strand-to-alpha-helix and alpha-helix-to-beta-strand transitions. These structural changes modulate catalysis and are promoted by interactions of the protein with anionic phospholipids in the membrane. | ||
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| - | Secondary structure reshuffling modulates glycosyltransferase function at the membrane.,Giganti D, Albesa-Jove D, Urresti S, Rodrigo-Unzueta A, Martinez MA, Comino N, Barilone N, Bellinzoni M, Chenal A, Guerin ME, Alzari PM Nat Chem Biol. 2015 Jan;11(1):16-8. doi: 10.1038/nchembio.1694. Epub 2014 Nov 17. PMID:25402770<ref>PMID:25402770</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4n9w" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of phosphatidyl mannosyltransferase PimA
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