1ds1

<StructureSection load='1ds1' size='340' side='right' caption='[[1ds1]], [[Resolution|resolution]] 1.08&Aring;' scene=''>

<table><tr><td colspan='2'>[[1ds1]] 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=1DS1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DS1 FirstGlance]. <br>

</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=PGO:S-1,2-PROPANEDIOL'>PGO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1drt|1drt]], [[1dry|1dry]], [[1ds0|1ds0]]</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=1ds1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ds1 OCA], [http://pdbe.org/1ds1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ds1 RCSB], [http://www.ebi.ac.uk/pdbsum/1ds1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ds1 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1ds1" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: As 4 1611]]

[[Category: Baldwin, J E]]

[[Category: Harlos, K]]

[[Category: Ren, J]]

[[Category: Schofield, C J]]

[[Category: Stammers, D K]]

[[Category: Zhang, Z H]]

[[Category: Trifunctional enzyme]]