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1MB9

BETA-LACTAM SYNTHETASE COMPLEXED WITH ATP

Summary for 1MB9
Entry DOI10.2210/pdb1mb9/pdb
Related1JGT 1MBZ 1MC1
DescriptorBETA-LACTAM SYNTHETASE, MAGNESIUM ION, PYROPHOSPHATE 2-, ... (6 entities in total)
Functional Keywordsclavulanic acid, asparagine synthetase, beta-lactam synthetase, carboxyethyl arginine, deoxyguanidinoproclavaminic acid, hydrolase
Biological sourceStreptomyces clavuligerus
Total number of polymer chains2
Total formula weight110837.89
Authors
Miller, M.T.,Bachmann, B.O.,Townsend, C.A.,Rosenzweig, A.C. (deposition date: 2002-08-02, release date: 2002-10-23, Last modification date: 2024-02-14)
Primary citationMiller, M.T.,Bachmann, B.O.,Townsend, C.A.,Rosenzweig, A.C.
The catalytic cycle of beta -lactam synthetase observed by x-ray crystallographic snapshots
Proc.Natl.Acad.Sci.USA, 99:14752-14757, 2002
Cited by
PubMed Abstract: 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.
PubMed: 12409610
DOI: 10.1073/pnas.232361199
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.11 Å)
Structure validation

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