2FYF

Structure of a putative phosphoserine aminotransferase from Mycobacterium Tuberculosis

2FYF の概要

• エントリーDOI: 10.2210/pdb2fyf/pdb
• 分子名称: phosphoserine aminotransferase, SULFATE ION, TETRACHLOROPLATINATE(II), ... (6 entities in total)
• 機能のキーワード: plp-dependent enzyme, dimer, structural genomics, mycobacterium tuberculosis structural proteomics project, xmtb, transferase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 89290.77

構造登録者

Coulibaly, F.,Lassalle, E.,Baker, E.N.,Mycobacterium Tuberculosis Structural Proteomics Project (XMTB) (登録日: 2006-02-07, 公開日: 2007-01-16, 最終更新日: 2024-02-14)

主引用文献

Coulibaly, F.,Lassalle, E.,Baker, H.M.,Baker, E.N.
Structure of phosphoserine aminotransferase from Mycobacterium tuberculosis.
Acta Crystallogr.,Sect.D, 68:553-563, 2012

PubMed Abstract: Mycobacterium tuberculosis (Mtb), the causative agent of TB, remains a serious world health problem owing to limitations of the available drugs and the emergence of resistant strains. In this context, key biosynthetic enzymes from Mtb are attractive targets for the development of new therapeutic drugs. Here, the 1.5 Å resolution crystal structure of Mtb phosphoserine aminotransferase (MtbPSAT) in complex with its cofactor, pyridoxal 5'-phosphate (PLP), is reported. MtbPSAT is an essential enzyme in the biosynthesis of serine and in pathways of one-carbon metabolism. The structure shows that although the Mtb enzyme differs substantially in sequence from other PSAT enzymes, its fold is conserved and its PLP-binding site is virtually identical. Structural comparisons suggest that this site remains unchanged throughout the catalytic cycle. On the other hand, PSAT enzymes are obligate dimers in which the two active sites are located in the dimer interface and distinct differences in the MtbPSAT dimer are noted. These impact on the substrate-binding region and access channel and suggest options for the development of selective inhibitors.

PubMed: 22525753
DOI: 10.1107/S0907444912004829

実験手法

X-RAY DIFFRACTION (1.5 Å)