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Crystal structure of penicillin G acylase from the bro1 mutant strain of providencia rettgeri
The structure of the Bro1 penicillin G acylase has been solved at 2.5 Å resolution by molecular replacement and a tightly bound calcium ion coordinated by one residue from the α‐sub unit and five residues from the β‐subunit has been identified.
The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 DD-peptidase family.
Though the evolutionary distance may vary considerably, all these penicillin-interactive proteins and domains appear to be members of a single superfamily of active-site-serine enzymes distinct from the classical trypsin or subtilisin families.
Reconciliation of the X-ray and NMR structures of the thrombin-binding aptamer d(GGTTGGTGTGGTTGG).
The thrombin-binding aptamer d(GGTTGGTGTGGTTGG) is one of a family of DNA oligonucleotides that were identified by in vitro selection to bind specifically and with high affinity to thrombin. Two
On the origin of bacterial resistance to penicillin: comparison of a beta-lactamase and a penicillin target.
Significant similarity found by x-ray crystallography in the spatial arrangement of the elements of secondary structure provides strong support for earlier hypotheses that beta-lactamases arose from penicillin-sensitive D-alanyl-D-alanine-peptidases involved in bacterial wall peptidoglycan metabolism.
X-ray crystallography of the binding of the bacterial cell wall trisaccharide NAM-NAG-NAM to lysozyme
The X-ray structure of the non-hydrolysed13 trisaccharide NAM-NAG-NAM bound in subsites B, C, D is presented and it is shown that the interpretation of the 2.5-Å resolution difference map does not involve distortion of this residue in site D.
2.8-A Structure of penicillin-sensitive D-alanyl carboxypeptidase-transpeptidase from Streptomyces R61 and complexes with beta-lactams.
The crystallographic structure of the penicillin-sensitive D-alanyl carboxypeptidase-transpeptidases from Streptomyces R61 has been solved to 2.8-A resolution and the binding at a common site of three types of beta-lactam has been observed in Fourier difference maps.
Comparison of the sequences of class A beta-lactamases and of the secondary structure elements of penicillin-recognizing proteins
A unified nomenclature of secondary structure elements is proposed for all the penicillin-recognizing enzymes.