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| | ==Pantothenate kinase from Mycobacterium tuberculosis (MtPanK) in complex with AMPPCP and Pantothenate== | | ==Pantothenate kinase from Mycobacterium tuberculosis (MtPanK) in complex with AMPPCP and Pantothenate== |
| - | <StructureSection load='2zse' size='340' side='right' caption='[[2zse]], [[Resolution|resolution]] 2.50Å' scene=''> | + | <StructureSection load='2zse' size='340' side='right'caption='[[2zse]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2zse]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZSE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZSE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2zse]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZSE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZSE FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PAU:PANTOTHENOIC+ACID'>PAU</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]] 2.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gev|2gev]], [[2geu|2geu]], [[2get|2get]], [[2ges|2ges]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PAU:PANTOTHENOIC+ACID'>PAU</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">coaA (Rv1092c) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</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=2zse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zse OCA], [https://pdbe.org/2zse PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zse RCSB], [https://www.ebi.ac.uk/pdbsum/2zse PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zse 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/Pantothenate_kinase Pantothenate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.33 2.7.1.33] </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=2zse FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zse OCA], [http://pdbe.org/2zse PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zse RCSB], [http://www.ebi.ac.uk/pdbsum/2zse PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zse ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/COAA_MYCTU COAA_MYCTU] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Pantothenate kinase|Pantothenate kinase]] | + | *[[Pantothenate kinase 3D structures|Pantothenate kinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Pantothenate kinase]] | + | [[Category: Large Structures]] |
| - | [[Category: Chetnani, B]] | + | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: Das, S]] | + | [[Category: Chetnani B]] |
| - | [[Category: Kumar, P]] | + | [[Category: Das S]] |
| - | [[Category: Surolia, A]] | + | [[Category: Kumar P]] |
| - | [[Category: Vijayan, M]] | + | [[Category: Surolia A]] |
| - | [[Category: Atp-binding]]
| + | [[Category: Vijayan M]] |
| - | [[Category: Coa biosynthesis]]
| + | |
| - | [[Category: Coenzyme a biosynthesis]]
| + | |
| - | [[Category: Homodimer]]
| + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Nucleotide binding]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
2zse is a 1 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.5Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
COAA_MYCTU
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structures of complexes of Mycobacterium tuberculosis pantothenate kinase with the following ligands have been determined: (i) citrate; (ii) the nonhydrolysable ATP analogue AMPPCP and pantothenate (the initiation complex); (iii) ADP and phosphopantothenate resulting from phosphorylation of pantothenate by ATP in the crystal (the end complex); (iv) ATP and ADP, each with half occupancy, resulting from a quick soak of crystals in ATP (the intermediate complex); (v) CoA; (vi) ADP prepared by soaking and cocrystallization, which turned out to have identical structures, and (vii) ADP and pantothenate. Solution studies on CoA binding and catalytic activity have also been carried out. Unlike in the case of the homologous Escherichia coli enzyme, AMPPCP and ADP occupy different, though overlapping, locations in the respective complexes; the same is true of pantothenate in the initiation complex and phosphopantothenate in the end complex. The binding site of MtPanK is substantially preformed, while that of EcPanK exhibits considerable plasticity. The difference in the behaviour of the E. coli and M. tuberculosis enzymes could be explained in terms of changes in local structure resulting from substitutions. It is unusual for two homologous enzymes to exhibit such striking differences in action. Therefore, the results have to be treated with caution. However, the changes in the locations of ligands exhibited by M. tuberculosis pantothenate kinase are remarkable and novel.
Mycobacterium tuberculosis pantothenate kinase: possible changes in location of ligands during enzyme action.,Chetnani B, Das S, Kumar P, Surolia A, Vijayan M Acta Crystallogr D Biol Crystallogr. 2009 Apr;65(Pt 4):312-25. Epub 2009, Mar 19. PMID:19307712[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chetnani B, Das S, Kumar P, Surolia A, Vijayan M. Mycobacterium tuberculosis pantothenate kinase: possible changes in location of ligands during enzyme action. Acta Crystallogr D Biol Crystallogr. 2009 Apr;65(Pt 4):312-25. Epub 2009, Mar 19. PMID:19307712 doi:10.1107/S0907444909002170
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