3af2: Difference between revisions
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<StructureSection load='3af2' size='340' side='right'caption='[[3af2]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='3af2' size='340' side='right'caption='[[3af2]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3af2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3af2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AF2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AF2 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id=' | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3af2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3af2 OCA], [https://pdbe.org/3af2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3af2 RCSB], [https://www.ebi.ac.uk/pdbsum/3af2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3af2 ProSAT]</span></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=3af2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3af2 OCA], [https://pdbe.org/3af2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3af2 RCSB], [https://www.ebi.ac.uk/pdbsum/3af2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3af2 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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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mycobacterium tuberculosis H37Rv]] | ||
[[Category: Chetnani B]] | |||
[[Category: Chetnani | [[Category: Kumar P]] | ||
[[Category: Kumar | [[Category: Surolia A]] | ||
[[Category: Surolia | [[Category: Vijayan M]] | ||
[[Category: Vijayan | |||
Latest revision as of 17:23, 1 November 2023
Pantothenate kinase from Mycobacterium tuberculosis (MtPanK) in complex with AMPPCPPantothenate kinase from Mycobacterium tuberculosis (MtPanK) in complex with AMPPCP
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedKinetic measurements of enzyme activity indicate that type I pantothenate kinase from Mycobacterium tuberculosis has dual substrate specificity for ATP and GTP, unlike the enzyme from Escherichia coli, which shows a higher specificity for ATP. A molecular explanation for the difference in the specificities of the two homologous enzymes is provided by the crystal structures of the complexes of the M. tuberculosis enzyme with (1) GMPPCP and pantothenate, (2) GDP and phosphopantothenate, (3) GDP, (4) GDP and pantothenate, (5) AMPPCP, and (6) GMPPCP, reported here, and the structures of the complexes of the two enzymes involving coenzyme A and different adenyl nucleotides reported earlier. The explanation is substantially based on two critical substitutions in the amino acid sequence and the local conformational change resulting from them. The structures also provide a rationale for the movement of ligands during the action of the mycobacterial enzyme. Dual specificity of the type exhibited by this enzyme is rare. The change in locations of ligands during action, observed in the case of the M. tuberculosis enzyme, is unusual, so is the striking difference between two homologous enzymes in the geometry of the binding site, locations of ligands, and specificity. Furthermore, the dual specificity of the mycobacterial enzyme appears to have been caused by a biological necessity. M. tuberculosis pantothenate kinase: dual substrate specificity and unusual changes in ligand locations.,Chetnani B, Kumar P, Surolia A, Vijayan M J Mol Biol. 2010 Jul 9;400(2):171-85. Epub 2010 May 6. PMID:20451532[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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