1ds0
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1ds0 |SIZE=350|CAPTION= <scene name='initialview01'>1ds0</scene>, resolution 1.63Å | |PDB= 1ds0 |SIZE=350|CAPTION= <scene name='initialview01'>1ds0</scene>, resolution 1.63Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1drt|1DRT]], [[1dry|1DRY]], [[1ds1|1DS1]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ds0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ds0 OCA], [http://www.ebi.ac.uk/pdbsum/1ds0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ds0 RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Stammers, D K.]] | [[Category: Stammers, D K.]] | ||
[[Category: Zhang, Z H.]] | [[Category: Zhang, Z H.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: SO4]] | ||
[[Category: clavaminate synthase 1]] | [[Category: clavaminate synthase 1]] | ||
[[Category: jelly roll]] | [[Category: jelly roll]] | ||
| Line 35: | Line 36: | ||
[[Category: trifunctional enzyme]] | [[Category: trifunctional enzyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:47:31 2008'' |
Revision as of 16:47, 30 March 2008
| |||||||
| , resolution 1.63Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1DRT, 1DRY, 1DS1
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF CLAVAMINATE SYNTHASE
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
1DS0 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
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