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(New page: 200px<br /><applet load="1dry" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dry, resolution 1.40&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1dry.gif|left|200px]]<br /><applet load="1dry" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dry, resolution 1.40&Aring;" />
 
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'''CRYSTAL STRUCTURE OF CLAVAMINATE SYNTHASE IN COMPLEX WITH FE(II), 2-OXOGLUTARATE AND N-ALPHA-L-ACETYL ARGININE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF CLAVAMINATE SYNTHASE IN COMPLEX WITH FE(II), 2-OXOGLUTARATE AND N-ALPHA-L-ACETYL ARGININE==
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Clavaminate synthase (CAS), a remarkable Fe(II)/2-oxoglutarate oxygenase, catalyzes three separate oxidative reactions in the biosynthesis of, clavulanic acid, a clinically used inhibitor of serine beta-lactamases., The first CAS-catalyzed step (hydroxylation) is separated from the latter, two (oxidative cyclization/desaturation) by the action of an, amidinohydrolase. Here, we describe crystal structures of CAS in complex, with Fe(II), 2-oxoglutarate (2OG) and substrates, (N-alpha-acetyl-L-arginine and proclavaminic acid). They reveal how CAS, catalyzes formation of the clavam nucleus, via a process unprecedented in, synthetic organic chemistry, and suggest how it discriminates between, substrates and controls reaction of its highly reactive ferryl, intermediate. The presence of an unpredicted jelly roll beta-barrel core, in CAS implies divergent evolution within the family of 2OG and related, oxygenases. Comparison with other non-heme oxidases/oxygenases reveals, flexibility in the position which dioxygen ligates to the iron, in, contrast to the analogous heme-using enzymes.
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<StructureSection load='1dry' size='340' side='right'caption='[[1dry]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dry]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DRY 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]] 1.4&#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=AAG:N-ALPHA-L-ACETYL-ARGININE'>AAG</scene>, <scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1dry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dry OCA], [https://pdbe.org/1dry PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dry RCSB], [https://www.ebi.ac.uk/pdbsum/1dry PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dry ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAS1_STRCL CAS1_STRCL]
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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/dr/1dry_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=1dry 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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Clavaminate synthase (CAS), a remarkable Fe(II)/2-oxoglutarate oxygenase, catalyzes three separate oxidative reactions in the biosynthesis of clavulanic acid, a clinically used inhibitor of serine beta-lactamases. The first CAS-catalyzed step (hydroxylation) is separated from the latter two (oxidative cyclization/desaturation) by the action of an amidinohydrolase. Here, we describe crystal structures of CAS in complex with Fe(II), 2-oxoglutarate (2OG) and substrates (N-alpha-acetyl-L-arginine and proclavaminic acid). They reveal how CAS catalyzes formation of the clavam nucleus, via a process unprecedented in synthetic organic chemistry, and suggest how it discriminates between substrates and controls reaction of its highly reactive ferryl intermediate. The presence of an unpredicted jelly roll beta-barrel core in CAS implies divergent evolution within the family of 2OG and related oxygenases. Comparison with other non-heme oxidases/oxygenases reveals flexibility in the position which dioxygen ligates to the iron, in contrast to the analogous heme-using enzymes.
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==About this Structure==
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Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase.,Zhang Z, Ren J, Stammers DK, Baldwin JE, Harlos K, Schofield CJ Nat Struct Biol. 2000 Feb;7(2):127-33. PMID:10655615<ref>PMID:10655615</ref>
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1DRY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus] with AAG, FE2, SO4, AKG and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DRY 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 origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase., Zhang Z, Ren J, Stammers DK, Baldwin JE, Harlos K, Schofield CJ, Nat Struct Biol. 2000 Feb;7(2):127-33. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10655615 10655615]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1dry" 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: Streptomyces clavuligerus]]
[[Category: Streptomyces clavuligerus]]
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[[Category: Baldwin, J.E.]]
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[[Category: Baldwin JE]]
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[[Category: Harlos, K.]]
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[[Category: Harlos K]]
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[[Category: Ren, J.]]
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[[Category: Ren J]]
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[[Category: Schofield, C.J.]]
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[[Category: Schofield CJ]]
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[[Category: Stammers, D.K.]]
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[[Category: Stammers DK]]
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[[Category: Zhang, Z.H.]]
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[[Category: Zhang ZH]]
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[[Category: AAG]]
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[[Category: AKG]]
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[[Category: FE2]]
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[[Category: GOL]]
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[[Category: SO4]]
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[[Category: clavaminate synthase 1]]
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[[Category: oxygenase]]
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[[Category: trifunctional enzyme]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:32:03 2007''
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Current revision

CRYSTAL STRUCTURE OF CLAVAMINATE SYNTHASE IN COMPLEX WITH FE(II), 2-OXOGLUTARATE AND N-ALPHA-L-ACETYL ARGININE

PDB ID 1dry

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