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2c2i
From Proteopedia
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STRUCTURE AND FUNCTION OF RV0130, A CONSERVED HYPOTHETICAL PROTEIN FROM M.TUBERCULOSIS
Overview
A large fraction of the Mycobacterium tuberculosis genome codes for proteins of unknown function. We here report the structure of one of these proteins, Rv0130, solved to a resolution of 1.8 a. The Rv0130 monomer features a single hotdog fold composed of a highly curved beta-sheet on top of a long and a short alpha-helix. Two monomers in turn pack to form a double-hotdog-folded homodimer, similar to a large group of enzymes that use thiol esters as substrates. Rv0130 was found to contain a highly conserved R-specific hydratase motif buried deeply between the two monomers. Our biochemical studies show that the protein is able to hydrate a short trans-2-enoyl-coenzyme A moiety with a k(cat) of 1.1 x 10(2) sec(-1). The importance of the side chains of D40 and H45 for hydratase activity is demonstrated by site-directed mutagenesis. In contrast to many hotdog-folded proteins, a proline residue distorts the central helix of Rv0130. This distortion allows the creation of a long, curved tunnel, similar to the substrate-binding channels of long-chain eukaryotic hydratase 2 enzymes.
About this Structure
2C2I is a Single protein structure of sequence from Mycobacterium tuberculosis. Active as Enoyl-CoA hydratase, with EC number 4.2.1.17 Full crystallographic information is available from OCA.
Reference
Structure and function of Rv0130, a conserved hypothetical protein from Mycobacterium tuberculosis., Johansson P, Castell A, Jones TA, Backbro K, Protein Sci. 2006 Oct;15(10):2300-9. Epub 2006 Sep 8. PMID:16963641
Page seeded by OCA on Thu Feb 21 16:44:09 2008
Categories: Enoyl-CoA hydratase | Mycobacterium tuberculosis | Single protein | Backbro, K. | Castell, A. | Johansson, P. | Jones, T A. | SPINE, Structural Proteomics in Europe. | Conserved hypothetical protein | Hotdog | Hydratase | Lyase | Rv0130 | Spine | Structural genomics | Structural proteomics in europe | Tuberculosis
