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

@article{citeulike:5872635, 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 \r{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.}, author = {Johansson, Patrik and Castell, Alina and Jones, T. Alwyn and B\"{a}ckbro, Kristina}, citeulike-article-id = {5872635}, citeulike-linkout-0 = {http://dx.doi.org/10.1110/ps.062309306}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/16963641}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=16963641}, doi = {10.1110/ps.062309306}, issn = {0961-8368}, journal = {Protein science : a publication of the Protein Society}, keywords = {hydratase, structure, tb}, month = {October}, number = {10}, pages = {2300--2309}, posted-at = {2009-10-02 03:32:52}, priority = {2}, title = {Structure and function of Rv0130, a conserved hypothetical protein from Mycobacterium tuberculosis.}, url = {http://dx.doi.org/10.1110/ps.062309306}, volume = {15}, year = {2006} }

TY - JOUR ID - citeulike:5872635 L3 - citeulike-article-id:5872635 N2 - 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. IS - 10 JF - Protein science : a publication of the Protein Society SN - 0961-8368 EP - 2309 TI - Structure and function of Rv0130, a conserved hypothetical protein from Mycobacterium tuberculosis. VL - 15 SP - 2300 KW - hydratase KW - structure KW - tb AU - Johansson, Patrik AU - Castell, Alina AU - Jones, Alwyn AU - Bäckbro, Kristina PY - 2006/10// UR - http://dx.doi.org/10.1110/ps.062309306 ER -