1jgt
From Proteopedia
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|PDB= 1jgt |SIZE=350|CAPTION= <scene name='initialview01'>1jgt</scene>, resolution 1.95Å | |PDB= 1jgt |SIZE=350|CAPTION= <scene name='initialview01'>1jgt</scene>, resolution 1.95Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=CMA:N2-(CARBOXYETHYL)-L-ARGININE'>CMA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= 1901 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1901 Streptomyces clavuligerus]) | |GENE= 1901 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1901 Streptomyces clavuligerus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jgt OCA], [http://www.ebi.ac.uk/pdbsum/1jgt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jgt RCSB]</span> | ||
}} | }} | ||
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[[Category: Rosenzweig, A C.]] | [[Category: Rosenzweig, A C.]] | ||
[[Category: Townsend, C A.]] | [[Category: Townsend, C A.]] | ||
| - | [[Category: APC]] | ||
| - | [[Category: CMA]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: MG]] | ||
[[Category: ampcpp]] | [[Category: ampcpp]] | ||
[[Category: asparagine synthetase]] | [[Category: asparagine synthetase]] | ||
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[[Category: clavulanic acid]] | [[Category: clavulanic acid]] | ||
| - | ''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 21:33:25 2008'' |
Revision as of 18:33, 30 March 2008
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| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | 1901 (Streptomyces clavuligerus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF BETA-LACTAM SYNTHETASE
Overview
The enzyme beta-lactam synthetase (beta-LS) catalyzes the formation of the beta-lactam ring in clavulanic acid, a clinically important beta-lactamase inhibitor. Whereas the penicillin beta-lactam ring is generated by isopenicillin N synthase (IPNS) in the presence of ferrous ion and dioxygen, beta-LS uses ATP and Mg2+ as cofactors. According to sequence alignments, beta-LS is homologous to class B asparagine synthetases (AS-Bs), ATP/Mg2+-dependent enzymes that convert aspartic acid to asparagine. Here we report the first crystal structure of a beta-LS. The 1.95 A resolution structure of Streptomyces clavuligerus beta-LS provides a fully resolved view of the active site in which substrate, closely related ATP analog alpha,beta-methyleneadenosine 5'-triphosphate (AMP-CPP) and a single Mg2+ ion are present. A high degree of substrate preorganization is observed. Comparison to Escherichia coli AS-B reveals the evolutionary changes that have taken place in beta-LS that impede interdomain reaction, which is essential in AS-B, and that accommodate beta-lactam formation. The structural data provide the opportunity to alter the synthetic potential of beta-LS, perhaps leading to the creation of new beta-lactamase inhibitors and beta-lactam antibiotics.
About this Structure
1JGT is a Single protein structure of sequence from Streptomyces clavuligerus. Full crystallographic information is available from OCA.
Reference
Structure of beta-lactam synthetase reveals how to synthesize antibiotics instead of asparagine., Miller MT, Bachmann BO, Townsend CA, Rosenzweig AC, Nat Struct Biol. 2001 Aug;8(8):684-9. PMID:11473258
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