3TA6

Structure of Mycobacterium tuberculosis triosephosphate isomerase

3TA6 の概要

• エントリーDOI: 10.2210/pdb3ta6/pdb
• 関連するPDBエントリー: 3GVG 3TAO
• 分子名称: Triosephosphate isomerase, CITRATE ANION (3 entities in total)
• 機能のキーワード: isomerase
• 由来する生物種: Mycobacterium tuberculosis
• 細胞内の位置: Cytoplasm (By similarity): P66940
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56714.90

構造登録者

Connor, S.E.,Capodagli, G.C.,Deaton, M.K.,Pegan, S.D. (登録日: 2011-08-03, 公開日: 2011-11-30, 最終更新日: 2024-02-28)

主引用文献

Connor, S.E.,Capodagli, G.C.,Deaton, M.K.,Pegan, S.D.
Structural and functional characterization of Mycobacterium tuberculosis triosephosphate isomerase.
Acta Crystallogr.,Sect.D, 67:1017-1022, 2011

PubMed Abstract: Tuberculosis (TB) is a major infectious disease that accounts for over 1.7 million deaths every year. Mycobacterium tuberculosis, the causative agent of tuberculosis, enters the human host by the inhalation of infectious aerosols. Additionally, one third of the world's population is likely to be infected with latent TB. The incidence of TB is on the rise owing in part to the emergence of multidrug-resistant strains. As a result, there is a growing need to focus on novel M. tuberculosis enzyme targets. M. tuberculosis triosephosphate isomerase (MtTPI) is an essential enzyme for gluconeogenetic pathways, making it a potential target for future therapeutics. In order to determine its structure, the X-ray crystal structure of MtTPI has been determined, as well as that of MtTPI bound with a reaction-intermediate analog. As a result, two forms of the active site were revealed. In conjunction with the kinetic parameters obtained for the MtTPI-facilitated conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (D-GAP), this provides a greater structural and biochemical understanding of this enzyme. Additionally, isothermal titration calorimetry was used to determine the binding constant for a reaction-intermediate analog bound to the active site of MtTPI.

PubMed: 22120738
DOI: 10.1107/S0907444911042971

実験手法

X-RAY DIFFRACTION (1.41 Å)