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1o8u

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[[Image:1o8u.gif|left|200px]]<br />
 
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<applet load="1o8u" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1o8u, resolution 2.00&Aring;" />
 
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'''THE 2 ANGSTROM STRUCTURE OF 6-OXO CAMPHOR HYDROLASE: NEW STRUCTURAL DIVERSITY IN THE CROTONASE SUPERFAMILY'''<br />
 
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==Overview==
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==The 2 Angstrom Structure of 6-Oxo Camphor Hydrolase: New Structural Diversity in the Crotonase Superfamily==
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6-Oxo camphor hydrolase (OCH) is an enzyme of the crotonase superfamily, that catalyzes carbon-carbon bond cleavage in bicyclic beta-diketones via, a retro-Claisen reaction (Grogan, G., Roberts, G. A., Bougioukou, D., Turner, N. J., and Flitsch, S. L. (2001) J. Biol. Chem. 276, 12565-12572)., The native structure of OCH has been solved at 2.0-A resolution with, selenomethionine multiple wave anomalous dispersion and refined to a final, R(free) of 19.0. The structure of OCH consists of a dimer of trimers that, resembles the "parent" enzyme of the superfamily, enoyl-CoA hydratase. In, contrast to enoyl-CoA hydratase, however, two octahedrally coordinated, sodium atoms are found at the 3-fold axis of the hexamer of OCH, and the, C-terminal helix of OCH does not form a discrete domain. Models of the, substrate, 6-oxo camphor, and a proposed enolate intermediate in the, putative active site suggest possible mechanistic roles for Glu-244, Asp-154, His-122, His-45, and His-145.
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<StructureSection load='1o8u' size='340' side='right'caption='[[1o8u]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1o8u]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O8U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O8U FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1o8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o8u OCA], [https://pdbe.org/1o8u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o8u RCSB], [https://www.ebi.ac.uk/pdbsum/1o8u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o8u ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAMK_RHOSO CAMK_RHOSO] Catalyzes the carbon-carbon bond cleavage of the bicyclic beta-diketone 6-oxocamphor via a retro-Claisen reaction to yield the optically active (2R,4S)-beta-campholinic acid. It is also able to cleave 2,2-disubstituted cyclohexa-1,3-diones such as 2-methyl-2-propylcyclohexa-1,3-dione and 2-methyl-2-butylcyclohexa-1,3-dione which result in racemic keto acid products. Transformations of the bicyclic diketone substrates bicyclo[2.2.1]heptane 2,6-dione and bicyclo[2.2.2]octane-2,6-dione yield (S)-keto acid products.<ref>PMID:11278926</ref> <ref>PMID:15138275</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o8/1o8u_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1o8u ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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6-Oxo camphor hydrolase (OCH) is an enzyme of the crotonase superfamily that catalyzes carbon-carbon bond cleavage in bicyclic beta-diketones via a retro-Claisen reaction (Grogan, G., Roberts, G. A., Bougioukou, D., Turner, N. J., and Flitsch, S. L. (2001) J. Biol. Chem. 276, 12565-12572). The native structure of OCH has been solved at 2.0-A resolution with selenomethionine multiple wave anomalous dispersion and refined to a final R(free) of 19.0. The structure of OCH consists of a dimer of trimers that resembles the "parent" enzyme of the superfamily, enoyl-CoA hydratase. In contrast to enoyl-CoA hydratase, however, two octahedrally coordinated sodium atoms are found at the 3-fold axis of the hexamer of OCH, and the C-terminal helix of OCH does not form a discrete domain. Models of the substrate, 6-oxo camphor, and a proposed enolate intermediate in the putative active site suggest possible mechanistic roles for Glu-244, Asp-154, His-122, His-45, and His-145.
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==About this Structure==
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The 2-A crystal structure of 6-oxo camphor hydrolase. New structural diversity in the crotonase superfamily.,Whittingham JL, Turkenburg JP, Verma CS, Walsh MA, Grogan G J Biol Chem. 2003 Jan 17;278(3):1744-50. Epub 2002 Nov 5. PMID:12421807<ref>PMID:12421807</ref>
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1O8U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis] with NA as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O8U OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The 2-A crystal structure of 6-oxo camphor hydrolase. New structural diversity in the crotonase superfamily., Whittingham JL, Turkenburg JP, Verma CS, Walsh MA, Grogan G, J Biol Chem. 2003 Jan 17;278(3):1744-50. Epub 2002 Nov 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12421807 12421807]
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</div>
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<div class="pdbe-citations 1o8u" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Rhodococcus erythropolis]]
[[Category: Rhodococcus erythropolis]]
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[[Category: Single protein]]
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[[Category: Grogan G]]
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[[Category: Grogan, G.]]
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[[Category: Turkenburg JP]]
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[[Category: Turkenburg, J.P.]]
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[[Category: Verma CS]]
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[[Category: Verma, C.S.]]
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[[Category: Walsh MA]]
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[[Category: Walsh, M.A.]]
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[[Category: Whittingham JL]]
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[[Category: Whittingham, J.L.]]
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[[Category: NA]]
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[[Category: crotonase]]
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[[Category: hydrolase]]
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[[Category: rhodococcuse]]
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[[Category: terpene metabolism]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:00:14 2007''
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Current revision

The 2 Angstrom Structure of 6-Oxo Camphor Hydrolase: New Structural Diversity in the Crotonase Superfamily

PDB ID 1o8u

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