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| | <StructureSection load='4nc9' size='340' side='right'caption='[[4nc9]], [[Resolution|resolution]] 3.19Å' scene=''> | | <StructureSection load='4nc9' size='340' side='right'caption='[[4nc9]], [[Resolution|resolution]] 3.19Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4nc9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycs2 Mycs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NC9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NC9 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4nc9]] is a 4 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=4NC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NC9 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n9w|4n9w]]</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]] 3.192Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MSMEG_2935, MSMEI_2861, pimA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2])</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=4nc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nc9 OCA], [https://pdbe.org/4nc9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nc9 RCSB], [https://www.ebi.ac.uk/pdbsum/4nc9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nc9 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.57 2.4.1.57] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nc9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nc9 OCA], [http://pdbe.org/4nc9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nc9 RCSB], [http://www.ebi.ac.uk/pdbsum/4nc9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nc9 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mycs2]] | + | [[Category: Mycolicibacterium smegmatis MC2 155]] |
| - | [[Category: Transferase]]
| + | [[Category: Albesa-Jove D]] |
| - | [[Category: Albesa-Jove, D]] | + | [[Category: Alzari PM]] |
| - | [[Category: Alzari, P M]] | + | [[Category: Bellinzoni M]] |
| - | [[Category: Bellinzoni, M]] | + | [[Category: Giganti D]] |
| - | [[Category: Giganti, D]] | + | [[Category: Guerin ME]] |
| - | [[Category: Guerin, M E]] | + | |
| - | [[Category: Gt-b]]
| + | |
| Structural highlights
Function
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.[1] [2]
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kordulakova J, Gilleron M, Mikusova K, Puzo G, Brennan PJ, Gicquel B, Jackson M. Definition of the first mannosylation step in phosphatidylinositol mannoside synthesis. PimA is essential for growth of mycobacteria. J Biol Chem. 2002 Aug 30;277(35):31335-44. Epub 2002 Jun 14. PMID:12068013 doi:10.1074/jbc.M204060200
- ↑ Guerin ME, Kaur D, Somashekar BS, Gibbs S, Gest P, Chatterjee D, Brennan PJ, Jackson M. New insights into the early steps of phosphatidylinositol mannoside biosynthesis in mycobacteria: PimB' is an essential enzyme of Mycobacterium smegmatis. J Biol Chem. 2009 Sep 18;284(38):25687-96. doi: 10.1074/jbc.M109.030593. Epub, 2009 Jul 28. PMID:19638342 doi:http://dx.doi.org/10.1074/jbc.M109.030593
- ↑ Giganti D, Albesa-Jove D, Urresti S, Rodrigo-Unzueta A, Martinez MA, Comino N, Barilone N, Bellinzoni M, Chenal A, Guerin ME, Alzari PM. Secondary structure reshuffling modulates glycosyltransferase function at the membrane. Nat Chem Biol. 2015 Jan;11(1):16-8. doi: 10.1038/nchembio.1694. Epub 2014 Nov 17. PMID:25402770 doi:http://dx.doi.org/10.1038/nchembio.1694
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