1jgt: Difference between revisions
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[[Image:1jgt.gif|left|200px]] | [[Image:1jgt.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF BETA-LACTAM SYNTHETASE''' | {{Structure | ||
|PDB= 1jgt |SIZE=350|CAPTION= <scene name='initialview01'>1jgt</scene>, resolution 1.95Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=CMA:N2-(CARBOXYETHYL)-L-ARGININE'>CMA</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= | |||
|GENE= 1901 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1901 Streptomyces clavuligerus]) | |||
}} | |||
'''CRYSTAL STRUCTURE OF BETA-LACTAM SYNTHETASE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1JGT is a [ | 1JGT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JGT OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11473258 11473258] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces clavuligerus]] | [[Category: Streptomyces clavuligerus]] | ||
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[[Category: clavulanic acid]] | [[Category: clavulanic acid]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:03:14 2008'' | ||
Revision as of 10:03, 20 March 2008
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| 1jgt, resolution 1.95Å | |||||||||||||
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| Ligands: | MG, APC, CMA and GOL | ||||||||||||
| Gene: | 1901 (Streptomyces clavuligerus) | ||||||||||||
| 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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