3HYS

Structure of Rv0554 from Mycobacterium tuberculosis complexed with Malonic Acid

Summary for 3HYS

• Entry DOI: 10.2210/pdb3hys/pdb
• Related: 3E3A 3HSS 3HZO
• Descriptor: protein Rv0554, putative Bromoperoxidase, MALONIC ACID, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (6 entities in total)
• Functional Keywords: hydrolase, oxidoreductase, peroxidase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 2
• Total formula weight: 65319.71

Authors

Johnston, J.M.,Baker, E.N. (deposition date: 2009-06-23, release date: 2010-06-02, Last modification date: 2024-02-21)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)