2c2i

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Template:STRUCTURE 2c2i

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. 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 Sun Apr 13 08:18:47 2008