2j5s

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[[Image:2j5s.gif|left|200px]]<br />
 
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<applet load="2j5s" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2j5s, resolution 1.57&Aring;" />
 
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'''STRUCTURAL OF ABDH, A BETA-DIKETONE HYDROLASE FROM THE CYANOBACTERIUM ANABAENA SP. PCC 7120 BOUND TO (S)-3-OXOCYCLOHEXYL ACETIC ACID'''<br />
 
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==Overview==
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==Structural of ABDH, a beta-diketone hydrolase from the Cyanobacterium Anabaena sp. PCC 7120 bound to (S)-3-oxocyclohexyl acetic acid==
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The gene alr4455 from the well-studied cyanobacterium Anabaena sp. PCC, 7120 encodes a crotonase orthologue that displays beta-diketone hydrolase, activity. Anabaena beta-diketone hydrolase (ABDH), in common with, 6-oxocamphor hydrolase (OCH) from Rhodococcus sp. NCIMB 9784, catalyzes, the desymmetrization of bicyclo[2.2.2]octane-2,6-dione to yield, [(S)-3-oxocyclohexyl]acetic acid, a reaction unusual among the crotonase, superfamily as the substrate is not an acyl-CoA thioester. The structure, of ABDH has been determined to a resolution of 1.5 A in both native and, ligand-bound forms. ABDH forms a hexamer similar to OCH and features one, active site per enzyme monomer. The arrangement of side chains in the, active site indicates that while the catalytic chemistry may be conserved, in OCH orthologues, the structural determinants of substrate specificity, are different. In the active site of ligand-bound forms that had been, cocrystallized with the bicyclic diketone substrate, bicyclo[2.2.2]octane-2,6-dione was found the product of the asymmetric, enzymatic retro-Claisen reaction [(S)-3-oxocyclohexyl]acetic acid. The, structures of ABDH in both native and ligand-bound forms reveal further, details about structural variation and modes of coenzyme A-independent, activity within the crotonases and provide further evidence of a wider, suprafamily of enzymes that have recruited the crotonase fold for the, catalysis of reactions other than those regularly attributed to canonical, superfamily members.
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<StructureSection load='2j5s' size='340' side='right'caption='[[2j5s]], [[Resolution|resolution]] 1.57&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2j5s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J5S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J5S 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]] 1.57&#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=KTA:(S)-CYCLOHEXANONE-2-ACETATE'>KTA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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=2j5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j5s OCA], [https://pdbe.org/2j5s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j5s RCSB], [https://www.ebi.ac.uk/pdbsum/2j5s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j5s ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8YNV6_NOSS1 Q8YNV6_NOSS1]
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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/j5/2j5s_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=2j5s 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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The gene alr4455 from the well-studied cyanobacterium Anabaena sp. PCC 7120 encodes a crotonase orthologue that displays beta-diketone hydrolase activity. Anabaena beta-diketone hydrolase (ABDH), in common with 6-oxocamphor hydrolase (OCH) from Rhodococcus sp. NCIMB 9784, catalyzes the desymmetrization of bicyclo[2.2.2]octane-2,6-dione to yield [(S)-3-oxocyclohexyl]acetic acid, a reaction unusual among the crotonase superfamily as the substrate is not an acyl-CoA thioester. The structure of ABDH has been determined to a resolution of 1.5 A in both native and ligand-bound forms. ABDH forms a hexamer similar to OCH and features one active site per enzyme monomer. The arrangement of side chains in the active site indicates that while the catalytic chemistry may be conserved in OCH orthologues, the structural determinants of substrate specificity are different. In the active site of ligand-bound forms that had been cocrystallized with the bicyclic diketone substrate bicyclo[2.2.2]octane-2,6-dione was found the product of the asymmetric enzymatic retro-Claisen reaction [(S)-3-oxocyclohexyl]acetic acid. The structures of ABDH in both native and ligand-bound forms reveal further details about structural variation and modes of coenzyme A-independent activity within the crotonases and provide further evidence of a wider suprafamily of enzymes that have recruited the crotonase fold for the catalysis of reactions other than those regularly attributed to canonical superfamily members.
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==About this Structure==
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Structural characterization of a beta-diketone hydrolase from the cyanobacterium Anabaena sp. PCC 7120 in native and product-bound forms, a coenzyme A-independent member of the crotonase suprafamily.,Bennett JP, Whittingham JL, Brzozowski AM, Leonard PM, Grogan G Biochemistry. 2007 Jan 9;46(1):137-44. PMID:17198383<ref>PMID:17198383</ref>
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2J5S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with NI and KTA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Beta-diketone_hydrolase Beta-diketone hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.7.1.7 3.7.1.7] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2J5S 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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Structural characterization of a beta-diketone hydrolase from the cyanobacterium Anabaena sp. PCC 7120 in native and product-bound forms, a coenzyme A-independent member of the crotonase suprafamily., Bennett JP, Whittingham JL, Brzozowski AM, Leonard PM, Grogan G, Biochemistry. 2007 Jan 9;46(1):137-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17198383 17198383]
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</div>
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[[Category: Anabaena sp.]]
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<div class="pdbe-citations 2j5s" style="background-color:#fffaf0;"></div>
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[[Category: Beta-diketone hydrolase]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Bennett, J.P.]]
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__TOC__
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[[Category: Brzozowski, A.M.]]
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</StructureSection>
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[[Category: Grogan, G.]]
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[[Category: Large Structures]]
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[[Category: Leonard, P.M.]]
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[[Category: Nostoc sp. PCC 7120 = FACHB-418]]
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[[Category: Whittingham, J.L.]]
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[[Category: Bennett JP]]
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[[Category: KTA]]
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[[Category: Brzozowski AM]]
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[[Category: NI]]
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[[Category: Grogan G]]
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[[Category: beta-diketone]]
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[[Category: Leonard PM]]
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[[Category: biocatalysis]]
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[[Category: Whittingham JL]]
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[[Category: c-c bond hydrolase]]
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[[Category: crotonase]]
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[[Category: enzyme evolution]]
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[[Category: hydrolase]]
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[[Category: lyase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:19:59 2007''
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Current revision

Structural of ABDH, a beta-diketone hydrolase from the Cyanobacterium Anabaena sp. PCC 7120 bound to (S)-3-oxocyclohexyl acetic acid

PDB ID 2j5s

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