2WU8

Structural studies of phosphoglucose isomerase from Mycobacterium tuberculosis H37Rv

2WU8 の概要

• エントリーDOI: 10.2210/pdb2wu8/pdb
• 分子名称: GLUCOSE-6-PHOSPHATE ISOMERASE, SULFATE ION (3 entities in total)
• 機能のキーワード: gluconeogenesis, 5-phosphoarabinonate (pab), pgi, isomerase, cytoplasm, glycolysis
• 由来する生物種: MYCOBACTERIUM TUBERCULOSIS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59784.72

構造登録者

Anand, K. (登録日: 2009-10-01, 公開日: 2009-10-27, 最終更新日: 2023-12-20)

主引用文献

Anand, K.,Mathur, D.,Anant, A.,Garg, L.C.
Structural Studies of Phosphoglucose Isomerase from Mycobacterium Tuberculosis H37Rv
Acta Crystallogr.,Sect.F, 66:490-, 2010

PubMed Abstract: Phosphoglucose isomerase (PGI) plays a key role in both glycolysis and gluconeogenesis inside the cell, whereas outside the cell it exhibits cytokine properties. PGI is also known to act as an autocrine motility factor, a neuroleukin agent and a differentiation and maturation mediator. Here, the first crystal structure of PGI from Mycobacterium tuberculosis H37Rv (Mtb) is reported. The structure was refined at 2.25 A resolution and revealed the presence of one molecule in the asymmetric unit with two globular domains. As known previously, the active site of Mtb PGI contains conserved residues including Glu356, Glu216 and His387 (where His387 is from the neighbouring molecule). The crystal structure of Mtb PGI was observed to be rather more similar to human PGI than other nonbacterial PGIs, with only a few differences being detected in the loops, arm and hook regions of the human and Mtb PGIs, suggesting that the M. tuberculosis enzyme uses the same enzyme mechanism.

PubMed: 20445242
DOI: 10.1107/S1744309110011656

実験手法

X-RAY DIFFRACTION (2.25 Å)