1q15
From Proteopedia
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'''Carbapenam Synthetase''' | '''Carbapenam Synthetase''' | ||
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[[Category: Stapon, A.]] | [[Category: Stapon, A.]] | ||
[[Category: Townsend, C A.]] | [[Category: Townsend, C A.]] | ||
| - | [[Category: | + | [[Category: A,b-methyleneadenosine 5-triphosphate]] |
| - | + | [[Category: Amp-cpp]] | |
| - | [[Category: | + | [[Category: As-b]] |
| - | [[Category: | + | [[Category: B-lactam synthetase]] |
| - | [[Category: | + | [[Category: B-l]] |
| - | [[Category: | + | [[Category: Cea]] |
| - | [[Category: | + | [[Category: Class b asparagine synthetase]] |
| - | [[Category: | + | [[Category: Cma]] |
| - | [[Category: | + | [[Category: Cmpr]] |
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Revision as of 02:44, 3 May 2008
Carbapenam Synthetase
Overview
Carbapenam synthetase (CarA) is an ATP/Mg2+-dependent enzyme that catalyzes formation of the beta-lactam ring in (5R)-carbapenem-3-carboxylic acid biosynthesis. CarA is homologous to beta-lactam synthetase (beta-LS), which is involved in clavulanic acid biosynthesis. The catalytic cycles of CarA and beta-LS mediate substrate adenylation followed by beta-lactamization via a tetrahedral intermediate or transition state. Another member of this family of ATP/Mg2+-dependent enzymes, asparagine synthetase (AS-B), catalyzes intermolecular, rather than intramolecular, amide bond formation in asparagine biosynthesis. The crystal structures of apo-CarA and CarA complexed with the substrate (2S,5S)-5-carboxymethylproline (CMPr), ATP analog alpha,beta-methyleneadenosine 5'-triphosphate (AMP-CPP), and a single Mg2+ ion have been determined. CarA forms a tetramer. Each monomer resembles beta-LS and AS-B in overall fold, but key differences are observed. The N-terminal domain lacks the glutaminase active site found in AS-B, and an extended loop region not observed in beta-LS or AS-B is present. Comparison of the C-terminal synthetase active site to that in beta-LS reveals that the ATP binding site is highly conserved. By contrast, variations in the substrate binding pocket reflect the different substrates of the two enzymes. The Mg2+ coordination is also different. Several key residues in the active site are conserved between CarA and beta-LS, supporting proposed roles in beta-lactam formation. These data provide further insight into the structures of this class of enzymes and suggest that CarA might be a versatile target for protein engineering experiments aimed at developing improved production methods and new carbapenem antibiotics.
About this Structure
1Q15 is a Single protein structure of sequence from Pectobacterium carotovorum. Full crystallographic information is available from OCA.
Reference
Crystal structure of carbapenam synthetase (CarA)., Miller MT, Gerratana B, Stapon A, Townsend CA, Rosenzweig AC, J Biol Chem. 2003 Oct 17;278(42):40996-1002. Epub 2003 Jul 30. PMID:12890666 Page seeded by OCA on Sat May 3 05:44:24 2008
