1m1z
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= taxon:1901 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1901 Streptomyces clavuligerus]) | |GENE= taxon:1901 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1901 Streptomyces clavuligerus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1jgt|1JGT]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m1z OCA], [http://www.ebi.ac.uk/pdbsum/1m1z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m1z RCSB]</span> | ||
}} | }} | ||
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[[Category: deoxyguanidinoproclavaminic acid]] | [[Category: deoxyguanidinoproclavaminic 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 22:10:14 2008'' |
Revision as of 19:10, 30 March 2008
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| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | taxon:1901 (Streptomyces clavuligerus) | ||||||
| Related: | 1JGT
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BETA-LACTAM SYNTHETASE APO ENZYME
Overview
The catalytic cycle of the ATP/Mg(2+)-dependent enzyme beta-lactam synthetase (beta-LS) from Streptomyces clavuligerus has been observed through a series of x-ray crystallographic snapshots. Chemistry is initiated by the ordered binding of ATP/Mg(2+) and N(2)-(carboxyethyl)-l-arginine (CEA) to the apoenzyme. The apo and ATP/Mg(2+) structures described here, along with the previously described CEA.alpha,beta-methyleneadenosine 5'-triphosphate (CEA.AMP-CPP)/Mg(2+) structure, illuminate changes in active site geometry that favor adenylation. In addition, an acyladenylate intermediate has been trapped. The substrate analog N(2)-(carboxymethyl)-l-arginine (CMA) was adenylated by ATP in the crystal and represents a close structural analog of the previously proposed CEA-adenylate intermediate. Finally, the structure of the ternary product complex deoxyguanidinoproclavaminic acid (DGPC).AMP/PP(i)/Mg(2+) has been determined. The CMA-AMP/PP(i)/Mg(2+) and DGPC.AMP/PP(i)/Mg(2+) structures reveal interactions in the active site that facilitate beta-lactam formation. All of the ATP-bound structures differ from the previously described CEA.AMP-CPP/Mg(2+) structure in that two Mg(2+) ions are found in the active sites. These Mg(2+) ions play critical roles in both the adenylation and beta-lactamization reactions.
About this Structure
1M1Z is a Single protein structure of sequence from Streptomyces clavuligerus. Full crystallographic information is available from OCA.
Reference
The catalytic cycle of beta -lactam synthetase observed by x-ray crystallographic snapshots., Miller MT, Bachmann BO, Townsend CA, Rosenzweig AC, Proc Natl Acad Sci U S A. 2002 Nov 12;99(23):14752-7. Epub 2002 Oct 30. PMID:12409610
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