2c2i
From Proteopedia
(New page: 200px<br /><applet load="2c2i" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c2i, resolution 1.80Å" /> '''STRUCTURE AND FUNCTI...) |
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| - | [[Image:2c2i.jpg|left|200px]]<br /><applet load="2c2i" size=" | + | [[Image:2c2i.jpg|left|200px]]<br /><applet load="2c2i" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2c2i, resolution 1.80Å" /> | caption="2c2i, resolution 1.80Å" /> | ||
'''STRUCTURE AND FUNCTION OF RV0130, A CONSERVED HYPOTHETICAL PROTEIN FROM M.TUBERCULOSIS'''<br /> | '''STRUCTURE AND FUNCTION OF RV0130, A CONSERVED HYPOTHETICAL PROTEIN FROM M.TUBERCULOSIS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A large fraction of the Mycobacterium tuberculosis genome codes for | + | 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== | ==About this Structure== | ||
| - | 2C2I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Active as [http://en.wikipedia.org/wiki/Enoyl-CoA_hydratase Enoyl-CoA hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.17 4.2.1.17] Full crystallographic information is available from [http:// | + | 2C2I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Active as [http://en.wikipedia.org/wiki/Enoyl-CoA_hydratase Enoyl-CoA hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.17 4.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C2I OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Castell, A.]] | [[Category: Castell, A.]] | ||
[[Category: Johansson, P.]] | [[Category: Johansson, P.]] | ||
| - | [[Category: Jones, T | + | [[Category: Jones, T A.]] |
| - | [[Category: SPINE, Structural | + | [[Category: SPINE, Structural Proteomics in Europe.]] |
[[Category: conserved hypothetical protein]] | [[Category: conserved hypothetical protein]] | ||
[[Category: hotdog]] | [[Category: hotdog]] | ||
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[[Category: tuberculosis]] | [[Category: tuberculosis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:44:09 2008'' |
Revision as of 14:44, 21 February 2008
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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
