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4qjl

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==Crystal structure of M. ulcerans phosphopantetheinyl transferase MuPPT==
==Crystal structure of M. ulcerans phosphopantetheinyl transferase MuPPT==
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<StructureSection load='4qjl' size='340' side='right' caption='[[4qjl]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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<StructureSection load='4qjl' size='340' side='right'caption='[[4qjl]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4qjl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycua Mycua]. 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>
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<table><tr><td colspan='2'>[[4qjl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_ulcerans_Agy99 Mycobacterium ulcerans Agy99]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4QJL FirstGlance]. <br>
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</td></tr><tr id='ligand'><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></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qjk|4qjk]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MUL_2141, MuPPT, pptII, YP_906028 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=362242 MYCUA])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4qjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qjl OCA], [https://pdbe.org/4qjl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qjl RCSB], [https://www.ebi.ac.uk/pdbsum/4qjl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qjl ProSAT]</span></td></tr>
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<tr id='activity'><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>
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<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=4qjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qjl OCA], [http://pdbe.org/4qjl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qjl RCSB], [http://www.ebi.ac.uk/pdbsum/4qjl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qjl ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0PQD8_MYCUA A0PQD8_MYCUA]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4qjl" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Mycua]]
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[[Category: Large Structures]]
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[[Category: Burkart, M D]]
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[[Category: Mycobacterium ulcerans Agy99]]
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[[Category: Noel, J P]]
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[[Category: Burkart MD]]
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[[Category: Vickery, C R]]
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[[Category: Noel JP]]
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[[Category: Coa binding]]
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[[Category: Vickery CR]]
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[[Category: Phosphopantetheinyl transferase]]
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[[Category: Transferase]]
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Current revision

Crystal structure of M. ulcerans phosphopantetheinyl transferase MuPPT

PDB ID 4qjl

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