3avp

Pantothenate kinase from Mycobacterium tuberculosis (MtPanK) in complex with Pantothenol

spinqualitylabelsall models 3avp, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3avp 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 2.6Å Ligands: FLC, GOL, MV2, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function COAA_MYCTU Publication Abstract from PubMed Previous studies of complexes of Mycobacterium tuberculosis PanK (MtPanK) with nucleotide diphosphates and nonhydrolysable analogues of nucleoside triphosphates in the presence or the absence of pantothenate established that the enzyme has dual specificity for ATP and GTP, revealed the unusual movement of ligands during enzyme action and provided information on the effect of pantothenate on the location and conformation of the nucleotides at the beginning and the end of enzyme action. The X-ray analyses of the binary complexes of MtPanK with pantothenate, pantothenol and N-nonylpantothenamide reported here demonstrate that in the absence of nucleotide these ligands occupy, with a somewhat open conformation, a location similar to that occupied by phosphopantothenate in the `end' complexes, which differs distinctly from the location of pantothenate in the closed conformation in the ternary `initiation' complexes. The conformation and the location of the nucleotide were also different in the initiation and end complexes. An invariant arginine appears to play a critical role in the movement of ligands that takes place during enzyme action. The work presented here completes the description of the locations and conformations of nucleoside diphosphates and triphosphates and pantothenate in different binary and ternary complexes, and suggests a structural rationale for the movement of ligands during enzyme action. The present investigation also suggests that N-alkylpantothenamides could be phosphorylated by the enzyme in the same manner as pantothenate. Location and conformation of pantothenate and its derivatives in Mycobacterium tuberculosis pantothenate kinase: insights into enzyme action.,Chetnani B, Kumar P, Abhinav KV, Chhibber M, Surolia A, Vijayan M Acta Crystallogr D Biol Crystallogr. 2011 Sep;67(Pt 9):774-83. doi:, 10.1107/S0907444911024462. Epub 2011 Aug 9. PMID:21904030 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pantothenate kinase 3D structures

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