1w0d
THE HIGH RESOLUTION STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS LEUB (RV2995C)
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OverviewOverview
The crystal structure of the enzyme 3-isopropylmalate dehydrogenase, (IPMDH) from Mycobacterium tuberculosis (LeuB, Mtb-IPMDH, Rv2995c) without, substrate or co-factor was determined at 1.65 A resolution, which is the, highest resolution reported for an IPMDH to date. The crystals contain two, functional dimers in the asymmetric unit in an arrangement close to a, tetramer of D2 symmetry. Despite the absence of a substrate or inhibitor, bound to the protein, the structure of the monomer resembles the, previously observed closed form of the enzyme more closely than the open, form. A comparison with the substrate complex of IPMDH from Thiobacillus, ferrooxidans and the co-factor complex of the Thermus thermophilus enzyme, revealed a close relationship of the active-site architecture between the, various bacterial enzymes. The inhibitor O-isobutenyl oxalylhydroxamate, was found to bind to the active site of IPMDH in a mode similar to the, substrate isopropylmalate.
About this StructureAbout this Structure
1W0D is a Single protein structure of sequence from Mycobacterium tuberculosis with SO4 as ligand. Active as 3-isopropylmalate dehydrogenase, with EC number 1.1.1.85 Full crystallographic information is available from OCA.
ReferenceReference
The high-resolution Structure of LeuB (Rv2995c) from Mycobacterium tuberculosis., Singh RK, Kefala G, Janowski R, Mueller-Dieckmann C, von Kries JP, Weiss MS, J Mol Biol. 2005 Feb 11;346(1):1-11. Epub 2004 Dec 23. PMID:15663922
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