3E3A

The Structure of Rv0554 from Mycobacterium tuberculosis

3E3A の概要

• エントリーDOI: 10.2210/pdb3e3a/pdb
• 関連するPDBエントリー: 3HSS
• 分子名称: POSSIBLE PEROXIDASE BPOC, ACETATE ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• 機能のキーワード: alpha/beta hydrolase, oxidoreductase, peroxidase
• 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: 64745.25

構造登録者

Johnston, J.M.,Baker, E.N. (登録日: 2008-08-06, 公開日: 2009-06-23, 最終更新日: 2024-02-21)

主引用文献

Johnston, J.M.,Jiang, M.,Guo, Z.,Baker, E.N.
Structural and functional analysis of Rv0554 from Mycobacterium tuberculosis: testing a putative role in menaquinone biosynthesis.
Acta Crystallogr.,Sect.D, 66:909-917, 2010

PubMed Abstract: Mycobacterium tuberculosis, the cause of tuberculosis, is a devastating human pathogen against which new drugs are urgently needed. Enzymes from the biosynthetic pathway for menaquinone are considered to be valid drug targets. The protein encoded by the open reading frame Rv0554 has been expressed, purified and subjected to structural and functional analysis to test for a putative role in menaquinone biosynthesis. The crystal structure of Rv0554 has been solved and refined in two different space groups at 2.35 and 1.9 A resolution. The protein is dimeric, with an alpha/beta-hydrolase monomer fold. In each monomer, a large cavity adjacent to the catalytic triad is enclosed by a helical lid. Dimerization is mediated by the lid regions. Small-molecule additives used in crystallization bind in the active site, but no binding of ligands related to menaquinone biosynthesis could be detected and functional assays failed to support possible roles in menaquinone biosynthesis.

PubMed: 20693690
DOI: 10.1107/S0907444910025771

実験手法

X-RAY DIFFRACTION (2.35 Å)