3AF2
Pantothenate kinase from Mycobacterium tuberculosis (MtPanK) in complex with AMPPCP
Summary for 3AF2
| Entry DOI | 10.2210/pdb3af2/pdb |
| Related | 2ZS8 2ZS9 2ZSA 2ZSB 2ZSE 2ZSF 3AEZ 3AF0 3AF1 3AF3 3AF4 |
| Descriptor | Pantothenate kinase, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | transferase, homodimer, coa biosynthesis, nucleotide binding, atp-binding, kinase, nucleotide-binding |
| Biological source | Mycobacterium tuberculosis |
| Cellular location | Cytoplasm (By similarity): P63810 |
| Total number of polymer chains | 1 |
| Total formula weight | 37223.09 |
| Authors | Chetnani, B.,Kumar, P.,Surolia, A.,Vijayan, M. (deposition date: 2010-02-22, release date: 2010-05-26, Last modification date: 2023-11-01) |
| Primary citation | Chetnani, B.,Kumar, P.,Surolia, A.,Vijayan, M. M. tuberculosis pantothenate kinase: dual substrate specificity and unusual changes in ligand locations J.Mol.Biol., 400:171-185, 2010 Cited by PubMed Abstract: Kinetic 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. PubMed: 20451532DOI: 10.1016/j.jmb.2010.04.064 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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