1W0D

The high resolution structure of Mycobacterium tuberculosis LeuB (Rv2995c)

Summary for 1W0D

• Entry DOI: 10.2210/pdb1w0d/pdb
• Descriptor: 3-ISOPROPYLMALATE DEHYDROGENASE, SULFATE ION (3 entities in total)
• Functional Keywords: dehydrogenase, oxidoreductase, leucine biosynthesis, nad, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tb, tbsgc
• Biological source: MYCOBACTERIUM TUBERCULOSIS
• Total number of polymer chains: 4
• Total formula weight: 141836.41

Authors

Singh, R.K.,Kefala, G.,Janowski, R.,Mueller-Dieckmann, C.,Weiss, M.S.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2004-06-03, release date: 2004-12-14, Last modification date: 2024-05-08)

Primary citation

Singh, R.K.,Kefala, G.,Janowski, R.,Mueller-Dieckmann, C.,Von Kries, J.P.,Weiss, M.S.
The High Resolution Structure of Leub (Rv2995C) from Mycobacterium Tuberculosis
J.Mol.Biol., 346:1-, 2005

PubMed Abstract: 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.

PubMed: 15663922
DOI: 10.1016/J.JMB.2004.11.059

Experimental method

X-RAY DIFFRACTION (1.65 Å)