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2c2i

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

Structural highlights

2c2i is a 2 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2c2i"

@@ Line 1: / Line 1: @@
-==STRUCTURE AND FUNCTION OF RV0130, A CONSERVED HYPOTHETICAL PROTEIN FROM M.TUBERCULOSIS==
-<StructureSection load='2c2i' size='340' side='right' caption='[[2c2i]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+==Structure and function of Rv0130, a conserved hypothetical protein from M.tuberculosis==
+<StructureSection load='2c2i' size='340' side='right'caption='[[2c2i]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2c2i]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. 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]] 1.8&#8491;</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://www.rcsb.org/pdb/explore.do?structureId=2c2i RCSB], [http://www.ebi.ac.uk/pdbsum/2c2i PDBsum]</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>
+== Function ==
+[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c2/2c2i_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c2/2c2i_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2c2i ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 25: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2c2i" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Enoyl-CoA hydratase]]
+[[Category: Large Structures]]
-[[Category: Mycobacterium tuberculosis]]
+[[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]]
-[[Category: Rv0130]]
-[[Category: Spine]]
-[[Category: Structural genomic]]
-[[Category: Structural proteomics in europe]]
-[[Category: Tuberculosis]]

2c2i

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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