1jgt
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1jgt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jgt, resolution 1.95Å" /> '''CRYSTAL STRUCTURE OF...)
Next diff →
Revision as of 16:07, 20 November 2007
|
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 with MG, APC, CMA and GOL as ligands. 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
Page seeded by OCA on Tue Nov 20 18:14:30 2007
