1WCF

1.54 A CRYSTAL STRUCTURE OF RV3628, MYCOBACTERIUM TUBERCULOSIS INORGANIC PYROPHOSPHATASE (PPASE) AT PH7.0

1WCF の概要

• エントリーDOI: 10.2210/pdb1wcf/pdb
• 分子名称: INORGANIC PYROPHOSPHATASE, POTASSIUM ION, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: structural genomics, potassium, hydrolase
• 由来する生物種: MYCOBACTERIUM TUBERCULOSIS
• 細胞内の位置: Cytoplasm (By similarity): P65746
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19660.04

構造登録者

Benini, S.,Wilson, K.S. (登録日: 2004-11-13, 公開日: 2006-07-12, 最終更新日: 2023-12-13)

主引用文献

Benini, S.,Wilson, K.S.
Structure of the Mycobacterium Tuberculosis Soluble Inorganic Pyrophosphatase Rv3628 at Ph 7.0.
Acta Crystallogr.,Sect.F, 67:866-, 2011

PubMed Abstract: The 1.5 Å resolution crystal structure of the Mycobacterium tuberculosis soluble inorganic pyrophosphatase Rv3628 at pH 7.0 is reported. The M. tuberculosis and M. leprae genomes include genes for the only two family I inorganic pyrophosphatases known to contain two histidines in the active site. The role of these two residues in catalysis is not fully understood. Mutational and functional studies of the M. tuberculosis enzyme showed that His21 and His86 are not essential for pyrophosphate hydrolysis, but are responsible for a shift in the optimal pH for the reaction compared with the Escherichia coli enzyme. Comparison with the structure previously reported at pH 5.0 provides further insight into the role of the two histidines. Two potassium-binding sites are found as a result of the high potassium concentration in the mother liquor.

PubMed: 21821883
DOI: 10.1107/S1744309111023323

実験手法

X-RAY DIFFRACTION (1.54 Å)