5XLV

Mycobacterium tuberculosis Pantothenate kinase mutant F254A

5XLV の概要

• エントリーDOI: 10.2210/pdb5xlv/pdb
• 関連するPDBエントリー: 5XLW
• 分子名称: Pantothenate kinase, SULFATE ION, TETRAETHYLENE GLYCOL, ... (6 entities in total)
• 機能のキーワード: homodimer, coa biosynthesis, nucleotide binding, concerted movement, structural transformation, transferase
• 由来する生物種: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 74665.08

構造登録者

Paul, A.,Kumar, P.,Surolia, A.,Vijayan, M. (登録日: 2017-05-11, 公開日: 2018-05-16, 最終更新日: 2023-11-22)

主引用文献

Paul, A.,Kumar, P.,Surolia, A.,Vijayan, M.
Biochemical and structural studies of mutants indicate concerted movement of the dimer interface and ligand-binding region of Mycobacterium tuberculosis pantothenate kinase
Acta Crystallogr F Struct Biol Commun, 73:635-643, 2017

PubMed Abstract: Two point mutants and the corresponding double mutant of Mycobacterium tuberculosis pantothenate kinase have been prepared and biochemically and structurally characterized. The mutants were designed to weaken the affinity of the enzyme for the feedback inhibitor CoA. The mutants exhibit reduced activity, which can be explained in terms of their structures. The crystals of the mutants are not isomorphous to any of the previously analysed crystals of the wild-type enzyme or its complexes. The mycobacterial enzyme and its homologous Escherichia coli enzyme exhibit structural differences in their nucleotide complexes in the dimer interface and the ligand-binding region. In three of the four crystallographically independent mutant molecules the structure is similar to that in the E. coli enzyme. Although the mutants involve changes in the CoA-binding region, the dimer interface and the ligand-binding region move in a concerted manner, an observation which might be important in enzyme action. This work demonstrates that the structure of the mycobacterial enzyme can be transformed into a structure similar to that of the E. coli enzyme through minor perturbations without external influences such as those involving ligand binding.

PubMed: 29095158
DOI: 10.1107/S2053230X17015667

実験手法

X-RAY DIFFRACTION (1.8 Å)