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1drt

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<StructureSection load='1drt' size='340' side='right'caption='[[1drt]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1drt' size='340' side='right'caption='[[1drt]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1drt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1611 As 4.1611]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DRT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DRT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1drt]] 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=1DRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DRT FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=PCV:5-AMINO-3-HYDROXY-2-(2-OXO-AZETIDIN-1-YL)-PENTANOIC+ACID'>PCV</scene></td></tr>
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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]] 2.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dry|1dry]], [[1ds0|1ds0]], [[1ds1|1ds1]]</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=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=PCV:5-AMINO-3-HYDROXY-2-(2-OXO-AZETIDIN-1-YL)-PENTANOIC+ACID'>PCV</scene></td></tr>
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<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=1drt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1drt OCA], [http://pdbe.org/1drt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1drt RCSB], [http://www.ebi.ac.uk/pdbsum/1drt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1drt ProSAT]</span></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=1drt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1drt OCA], [https://pdbe.org/1drt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1drt RCSB], [https://www.ebi.ac.uk/pdbsum/1drt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1drt ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CAS1_STRCL CAS1_STRCL]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1drt 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=1drt ConSurf].
<div style="clear:both"></div>
<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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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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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1drt" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: As 4 1611]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Baldwin, J E]]
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[[Category: Streptomyces clavuligerus]]
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[[Category: Harlos, K]]
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[[Category: Baldwin JE]]
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[[Category: Ren, J]]
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[[Category: Harlos K]]
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[[Category: Schofield, C J]]
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[[Category: Ren J]]
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[[Category: Stammers, D K]]
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[[Category: Schofield CJ]]
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[[Category: Zhang, Z H]]
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[[Category: Stammers DK]]
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[[Category: Clavaminate synthase 1]]
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[[Category: Zhang ZH]]
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[[Category: Lyase]]
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[[Category: Oxidoreductase]]
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[[Category: Oxygenase]]
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[[Category: Trifunctional enzyme]]
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Current revision

CRYSTAL STRUCTURE OF CLAVAMINATE SYNTHASE IN COMPLEX WITH FE(II), 2-OXOGLUTARATE AND PROCLAVAMINIC ACID

PDB ID 1drt

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