Identification of the active site in penicillin-binding protein 3 of Escherichia coli.
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Nicholas RA, Strominger JL, Suzuki H, Hirota Y
Identification of the active site in penicillin-binding protein 3 of Escherichia coli.
J Bacteriol. 1985 Oct;164(1):456-60.
- PubMed ID
- 3900044 [ View in PubMed]
- Abstract
We report the sequence of the active site tryptic peptide of penicillin-binding protein 3 from Escherichia coli. Purified penicillin-binding protein 3 was labeled with [14C]penicillin G and digested with trypsin, and the resulting radioactive peptides were isolated by a combination of gel filtration and high-pressure liquid chromatography. The major radioactive peak from high-pressure liquid chromatography was sequenced, and the peptide Thr-Ile-Thr-Asp-Val-Phe-Glu-Pro-Gly-Ser-Thr-Val-Lys, which comprises residues 298 to 310 in the amino acid sequence, was identified. This sequence is compared with the active site sequences from other penicillin-binding proteins and beta-lactamases.