1ds1

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[[Image:1ds1.gif|left|200px]]
[[Image:1ds1.gif|left|200px]]
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{{Structure
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|PDB= 1ds1 |SIZE=350|CAPTION= <scene name='initialview01'>1ds1</scene>, resolution 1.08&Aring;
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The line below this paragraph, containing "STRUCTURE_1ds1", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=AKG:2-OXYGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=PGO:1,2-PROPANEDIOL'>PGO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1ds1| PDB=1ds1 | SCENE= }}
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|RELATEDENTRY=[[1drt|1DRT]], [[1dry|1DRY]], [[1ds0|1DS0]]
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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1ds1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ds1 RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF CLAVAMINATE SYNTHASE IN COMPLEX WITH FE(II) AND 2-OXOGLUTARATE'''
'''CRYSTAL STRUCTURE OF CLAVAMINATE SYNTHASE IN COMPLEX WITH FE(II) AND 2-OXOGLUTARATE'''
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[[Category: Stammers, D K.]]
[[Category: Stammers, D K.]]
[[Category: Zhang, Z H.]]
[[Category: Zhang, Z H.]]
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[[Category: clavaminate synthase 1]]
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[[Category: Clavaminate synthase 1]]
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[[Category: oxygenase]]
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[[Category: Oxygenase]]
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[[Category: trifunctional enzyme]]
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[[Category: Trifunctional enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:12:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:47:31 2008''
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Revision as of 11:12, 2 May 2008

Template:STRUCTURE 1ds1

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


Overview

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.

About this Structure

1DS1 is a Single protein structure of sequence from Streptomyces clavuligerus. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 14:12:11 2008

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