2C2I

Structure and function of Rv0130, a conserved hypothetical protein from M.tuberculosis

Summary for 2C2I

• Entry DOI: 10.2210/pdb2c2i/pdb
• Descriptor: RV0130 (2 entities in total)
• Functional Keywords: rv0130, tuberculosis, conserved hypothetical protein, hotdog, hydratase, lyase, structural proteomics in europe, spine, structural genomics
• Biological source: MYCOBACTERIUM TUBERCULOSIS
• Total number of polymer chains: 2
• Total formula weight: 32327.63

Authors

Johansson, P.,Castell, A.,Jones, T.A.,Backbro, K. (deposition date: 2005-09-29, release date: 2006-09-14, Last modification date: 2024-11-13)

Primary citation

Johansson, P.,Castell, A.,Jones, T.A.,Backbro, K.
Structure and Function of Rv0130, a Conserved Hypothetical Protein from Mycobacterium Tuberculosis.
Protein Sci., 15:2300-, 2006

PubMed Abstract: 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 å. 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.

PubMed: 16963641
DOI: 10.1110/PS.062309306

Experimental method

X-RAY DIFFRACTION (1.8 Å)