1jgt

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[[Image:1jgt.gif|left|200px]]
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{{STRUCTURE_1jgt| PDB=1jgt | SCENE= }}
{{STRUCTURE_1jgt| PDB=1jgt | SCENE= }}
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'''CRYSTAL STRUCTURE OF BETA-LACTAM SYNTHETASE'''
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===CRYSTAL STRUCTURE OF BETA-LACTAM SYNTHETASE===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_11473258}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11473258 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11473258}}
==About this Structure==
==About this Structure==
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[[Category: Cea]]
[[Category: Cea]]
[[Category: Clavulanic acid]]
[[Category: Clavulanic acid]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:12:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:13:25 2008''

Revision as of 17:13, 1 July 2008

Image:1jgt.png

Template:STRUCTURE 1jgt

CRYSTAL STRUCTURE OF BETA-LACTAM SYNTHETASE

Template:ABSTRACT PUBMED 11473258

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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