Title: Structural and functional analysis of Rv0554 from Mycobacterium tuberculosis: testing a putative role in menaquinone biosynthesis Johnston JM, Jiang M, Guo Z, Baker EN Ref: Acta Crystallographica D Biol Crystallogr, 66:909, 2010 : PubMed
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.
Representative scheme of 6_AlphaBeta_hydrolase structure and an image from PDBsum server
no Image
Databases
PDB-Sum
3HZO Previously Class, Architecture, Topology and Homologous superfamily - PDB-Sum server
FSSP
3HZOFold classification based on Structure-Structure alignment of Proteins - FSSP server
