3AEZ

Pantothenate kinase from Mycobacterium tuberculosis (MtPanK) in complex with GDP and Phosphopantothenate

3AEZ の概要

• エントリーDOI: 10.2210/pdb3aez/pdb
• 関連するPDBエントリー: 2ZS8 2ZS9 2ZSA 2ZSB 2ZSE 2ZSF 3AF0 3AF1 3AF2 3AF3 3AF4
• 分子名称: Pantothenate kinase, GUANOSINE-5'-DIPHOSPHATE, N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanine, ... (6 entities in total)
• 機能のキーワード: transferase, homodimer, coa biosynthesis, nucleotide binding, atp-binding, kinase, nucleotide-binding
• 由来する生物種: Mycobacterium tuberculosis
• 細胞内の位置: Cytoplasm (By similarity): P63810
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 37667.48

構造登録者

Chetnani, B.,Kumar, P.,Surolia, A.,Vijayan, M. (登録日: 2010-02-18, 公開日: 2010-05-26, 最終更新日: 2023-11-01)

主引用文献

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

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: 20451532
DOI: 10.1016/j.jmb.2010.04.064

実験手法

X-RAY DIFFRACTION (2.2 Å)