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Cited by 351

The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.

Bacterial Resistance to β-Lactam Antibiotics: Crystal Structure of β-Lactamase from Staphylococcus aureus PC1 at 2.5 Å Resolution

Herzberg, Osnat, Moult, John·1987·Science

Abstract

β-lactamases are enzymes that protect bacteria from the lethal effects of β-lactam antibiotics, and are therefore of considerable clinical importance. The crystal structure of β-lactamase from the Gram-positive bacterium Staphylococcus aureus PC1 has been determined at 2.5 angstrom resolution. It reveals a molecule of novel topology, made up of two closely associated domains. The active site is located at the interface between the domains, with the key catalytic residue Ser 70 at the amino terminus of a buried helix. Examination of the disposition of the functionally important residues within the active site depression leads to a model for the binding of a substrate and a functional analogy to the serine proteases. The unusual topology of the secondary structure units is relevant to questions concerning the evolutionary relation to the β-lactam target enzymes of the bacterial cell wall.

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Crossref · 10.1126/science.3107125

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Metadata

Authors
Herzberg, O., & Moult, J.
Venue
Science
Published
1987-05-08
Volume
236
Issue
4802
Pages
694-701
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2026130809
Cited by
351
References
29
FWCI
21.32
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Bacterial Resistance to β-Lactam Antibiotics: Crystal Structure of β-Lactamase from Staphylococcus aureus PC1 at 2.5 Å Resolution. https://app.cochat.ai/papers/10.1126/science.3107125
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Herzberg, O., & Moult, J. (1987). Bacterial Resistance to β-Lactam Antibiotics: Crystal Structure of β-Lactamase from Staphylococcus aureus PC1 at 2.5 Å Resolution. Science. https://doi.org/10.1126/science.3107125

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.