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| {{STRUCTURE_2c2i| PDB=2c2i | SCENE= }} | | {{STRUCTURE_2c2i| PDB=2c2i | SCENE= }} |
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| '''STRUCTURE AND FUNCTION OF RV0130, A CONSERVED HYPOTHETICAL PROTEIN FROM M.TUBERCULOSIS'''
| | ===STRUCTURE AND FUNCTION OF RV0130, A CONSERVED HYPOTHETICAL PROTEIN FROM M.TUBERCULOSIS=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16963641}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16963641 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16963641}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Structural proteomics in europe]] | | [[Category: Structural proteomics in europe]] |
| [[Category: Tuberculosis]] | | [[Category: Tuberculosis]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:18:47 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:59:31 2008'' |
