3oka
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of Corynebacterium glutamicum PimB' in complex with GDP-Man (triclinic crystal form)== | |
| - | + | <StructureSection load='3oka' size='340' side='right' caption='[[3oka]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3oka]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OKA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OKA FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDD:GUANOSINE-5-DIPHOSPHATE-ALPHA-D-MANNOSE'>GDD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3okc|3okc]], [[3okp|3okp]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pimB, Cgl2186, cg2400 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1718 Corynebacterium glutamicum]), His-affinity tag ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphatidylinositol_alpha-mannosyltransferase Phosphatidylinositol alpha-mannosyltransferase], 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=3oka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oka OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oka RCSB], [http://www.ebi.ac.uk/pdbsum/3oka PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ok/3oka_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Long term survival of the pathogen Mycobacterium tuberculosis in humans is linked to the immunomodulatory potential of its complex cell wall glycolipids, which include the phosphatidylinositol mannoside (PIM) series as well as the related lipomannan and lipoarabinomannan glycoconjugates. PIM bioynthesis is initiated by a set of cytosolic alpha-mannosyltransferases, catalysing glycosyl transfer from the activated saccharide donor GDP-Man to the acceptor phosphatidyl-myo-inositol (PI) in an ordered and regio-specific fashion. Herein, we report the crystal structure of mannosyltransferase C. glutamicum PimB' in complex with nucleotide to a resolution of 2.0 A. PimB' attaches mannosyl selectively to the 6-OH of the inositol moiety of PI. Two crystal forms and GDP- versus GDP-Man-bound complexes reveal flexibility of the nucleotide conformation as well as of the structural framework of the active site. Structural comparison, docking of the saccharide acceptor and site directed mutagenesis pin regio-selectivity to a conserved Asp residue in the N-terminal domain that forces presentation of the correct inositol hydroxyl to the saccharide donor. | ||
| - | + | Acceptor substrate discrimination in phosphatidyl-myo-inositol mannoside synthesis: Structural and mutational analysis of mannosyltransferase Corynebacterium glutamicum PimB',Batt SM, Jabeen T, Mishra AK, Veerapen N, Krumbach K, Eggeling L, Besra GS, Futterer K J Biol Chem. 2010 Sep 15. PMID:20843801<ref>PMID:20843801</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Corynebacterium glutamicum]] | [[Category: Corynebacterium glutamicum]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Phosphatidylinositol alpha-mannosyltransferase]] | [[Category: Phosphatidylinositol alpha-mannosyltransferase]] | ||
| - | [[Category: Batt, S M | + | [[Category: Batt, S M]] |
| - | [[Category: Besra, G S | + | [[Category: Besra, G S]] |
| - | [[Category: Futterer, K | + | [[Category: Futterer, K]] |
| - | [[Category: Jabeen, T | + | [[Category: Jabeen, T]] |
[[Category: Alpha-mannosyltransferase]] | [[Category: Alpha-mannosyltransferase]] | ||
[[Category: Gdp-man binding]] | [[Category: Gdp-man binding]] | ||
[[Category: Gt-b fold]] | [[Category: Gt-b fold]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 07:15, 19 December 2014
Crystal structure of Corynebacterium glutamicum PimB' in complex with GDP-Man (triclinic crystal form)
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