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| | <StructureSection load='2c2i' size='340' side='right'caption='[[2c2i]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='2c2i' size='340' side='right'caption='[[2c2i]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2c2i]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C2I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C2I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2c2i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C2I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C2I FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c2i OCA], [http://pdbe.org/2c2i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c2i RCSB], [http://www.ebi.ac.uk/pdbsum/2c2i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c2i ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c2i OCA], [https://pdbe.org/2c2i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c2i RCSB], [https://www.ebi.ac.uk/pdbsum/2c2i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c2i ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ECH1_MYCTO ECH1_MYCTO]] May be involved in the hydration of fatty acids for production of polyhydroxylalkanoates. | + | [https://www.uniprot.org/uniprot/HTDZ_MYCTU HTDZ_MYCTU] Shows trans-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydratase activity. In vitro, can hydrate (2E)-butenoyl-CoA, (2E)-hexenoyl-CoA and (2E)-decenoyl-CoA.<ref>PMID:16963641</ref> <ref>PMID:18375556</ref> <ref>PMID:19136596</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Enoyl-CoA hydratase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Myctu]] | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Backbro, K]] | + | [[Category: Backbro K]] |
| - | [[Category: Castell, A]] | + | [[Category: Castell A]] |
| - | [[Category: Johansson, P]] | + | [[Category: Johansson P]] |
| - | [[Category: Jones, T A]] | + | [[Category: Jones TA]] |
| - | [[Category: Conserved hypothetical protein]]
| + | |
| - | [[Category: Hotdog]]
| + | |
| - | [[Category: Hydratase]]
| + | |
| - | [[Category: Lyase]]
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| - | [[Category: Rv0130]]
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| - | [[Category: Spine]]
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| - | [[Category: Structural genomic]]
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| - | [[Category: Structural proteomics in europe]]
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| - | [[Category: Tuberculosis]]
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| Structural highlights
Function
HTDZ_MYCTU Shows trans-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydratase activity. In vitro, can hydrate (2E)-butenoyl-CoA, (2E)-hexenoyl-CoA and (2E)-decenoyl-CoA.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Johansson P, Castell A, Jones TA, Backbro K. Structure and function of Rv0130, a conserved hypothetical protein from Mycobacterium tuberculosis. Protein Sci. 2006 Oct;15(10):2300-9. Epub 2006 Sep 8. PMID:16963641 doi:10.1110/ps.062309306
- ↑ Gurvitz A, Hiltunen JK, Kastaniotis AJ. Identification of a novel mycobacterial 3-hydroxyacyl-thioester dehydratase, HtdZ (Rv0130), by functional complementation in yeast. J Bacteriol. 2008 Jun;190(11):4088-90. PMID:18375556 doi:10.1128/JB.00016-08
- ↑ Gurvitz A, Hiltunen JK, Kastaniotis AJ. Heterologous expression of mycobacterial proteins in Saccharomyces cerevisiae reveals two physiologically functional 3-hydroxyacyl-thioester dehydratases, HtdX and HtdY, in addition to HadABC and HtdZ. J Bacteriol. 2009 Apr;191(8):2683-90. doi: 10.1128/JB.01046-08. Epub 2009 Jan 9. PMID:19136596 doi:http://dx.doi.org/10.1128/JB.01046-08
- ↑ Johansson P, Castell A, Jones TA, Backbro K. Structure and function of Rv0130, a conserved hypothetical protein from Mycobacterium tuberculosis. Protein Sci. 2006 Oct;15(10):2300-9. Epub 2006 Sep 8. PMID:16963641 doi:10.1110/ps.062309306
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