4qjl
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==Crystal structure of M. ulcerans phosphopantetheinyl transferase MuPPT== |
| + | <StructureSection load='4qjl' size='340' side='right' caption='[[4qjl]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4qjl]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QJL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QJL FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qjk|4qjk]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Holo-[acyl-carrier-protein]_synthase Holo-[acyl-carrier-protein] synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.8.7 2.7.8.7] </span></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qjl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qjl RCSB], [http://www.ebi.ac.uk/pdbsum/4qjl PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 4'-Phosphopantetheinyl transferases (PPTase) post-translationally modify carrier proteins with a phosphopantetheine moiety, an essential reaction in all three domains of life. In the bacterial genus Mycobacteria, the Sfp-type PPTase activates pathways necessary for the biosynthesis of cell wall components and small molecule virulence factors. We solved the X-ray crystal structures and biochemically characterized the Sfp-type PPTases from two of the most prevalent Mycobacterial pathogens, PptT of M. tuberculosis and MuPPT of M. ulcerans. Structural analyses reveal significant differences in cofactor binding and active site composition when compared to previously characterized Sfp-type PPTases. Functional analyses including the efficacy of Sfp-type PPTase-specific inhibitors also suggest that the Mycobacterial Sfp-type PPTases can serve as therapeutic targets against Mycobacterial infections. | ||
| - | + | Structure, Biochemistry, and Inhibition of Essential 4'-Phosphopantetheinyl Transferases from Two Species of Mycobacteria.,Vickery CR, Kosa NM, Casavant EP, Duan S, Noel JP, Burkart MD ACS Chem Biol. 2014 Jul 9. PMID:24963544<ref>PMID:24963544</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Burkart, M D.]] | ||
| + | [[Category: Noel, J P.]] | ||
| + | [[Category: Vickery, C R.]] | ||
| + | [[Category: Coa binding]] | ||
| + | [[Category: Phosphopantetheinyl transferase]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 10:15, 16 July 2014
Crystal structure of M. ulcerans phosphopantetheinyl transferase MuPPT
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