2ZSD

Pantothenate kinase from Mycobacterium tuberculosis (MtPanK) in complex with Coenzyme A

2ZSD の概要

• エントリーDOI: 10.2210/pdb2zsd/pdb
• 関連するPDBエントリー: 2GES 2GET 2GEU 2GEV
• 分子名称: Pantothenate kinase, COENZYME A, GLYCEROL, ... (6 entities in total)
• 機能のキーワード: transferase, homodimer, coa biosynthesis, nucleotide binding, atp-binding, coenzyme a biosynthesis, kinase
• 由来する生物種: Mycobacterium tuberculosis
• 細胞内の位置: Cytoplasm (Probable): P63810
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38033.72

構造登録者

Chetnani, B.,Das, S.,Kumar, P.,Surolia, A.,Vijayan, M. (登録日: 2008-09-05, 公開日: 2009-07-21, 最終更新日: 2023-11-01)

主引用文献

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.,Sect.D, 65:312-325, 2009

PubMed Abstract: 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.

PubMed: 19307712
DOI: 10.1107/S0907444909002170

実験手法

X-RAY DIFFRACTION (2.5 Å)