The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Crystal structure of Escherichia coli TEM1 β‐lactamase at 1.8 Å resolution
Open accessAbstract
The X‐ray structure of Escherichia coli TEM1β‐lactamase has been refined to a crystallorgphic R‐factor of 16.4% for 22,510 reflections between 5.0 and 1.8 Å resolution; 199 water molecules and 1 sulphate ion were included in refinement. Except for the tips of a few solvent‐exposed side chains, all protein atoms have clear electron density and refined to an average atomic temperature factor of 11 Å 2. The estimated coordinates error is 0.17 Å. The substrate binding site is located at the interface of the two domains of the protein and contains 4 water molecules and the sulphate anion. One of these solvent molecules is found at hydrogen bond distance from S70 and E166. S70 and S130 are hydrogen bonded to K73 and K234, respectively. It was found that the E. coli TEM1 and Staphylococcus aureus PC1 β‐lactamases crystal structures differ in the relative orientations of the two domains composing the enzymes, which result in a narrowed substrate binding cavity in the TEM1 enzyme. Local but significant differences in the vicinity of this site may explain the occurrence of TEM1 natural mutants with extended substrate specificities. © 1993 Wiley‐Liss, Inc.
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Luzzati, V. (1952) · Acta Crystallographica · doi:10.1107/s0365110x52002161 · Cited by 1,251
A standard numbering scheme for the class A β-lactamases
Ambler, R. P., Coulson, A. F. W., Frère, J. M., Ghuysen, J. M., Joris, B., Forsman, M., Levesque, R. C., Tiraby, G., & Waley, S. G. (1991) · Biochemical Journal · doi:10.1042/bj2760269 · Cited by 1,073
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Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at 1.7 Å resolution
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Three Decades of β-Lactamase Inhibitors
Drawz, S. M., & Bonomo, R. A. (2010) · Clinical Microbiology Reviews · doi:10.1128/cmr.00037-09 · Cited by 1,709
The modular architecture of protein–protein binding interfaces
Reichmann, D., Rahat, O., Albeck, S., Meged, R., Dym, O., & Schreiber, G. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407280102 · Cited by 239
Zaccolo, M., & Gherardi, E. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2262 · Cited by 200
Metadata
- Authors
- Jelsch, C., Mourey, L., Masson, J., & Samama, J.
- Venue
- Proteins: Structure, Function, and Bioinformatics
- Publisher
- Wiley
- Published
- 1993-08
- Volume
- 16
- Issue
- 4
- Pages
- 364-383
- ISSN
- 0887-3585 (ISSN-L)
- 1097-0134
- OpenAlex
- W2147872249
- Cited by
- 357
- References
- 30
- FWCI
- 10.11
- Type
- journal article
- Language
- en
- Open access
- green
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- Jelsch, C., Mourey, L., Masson, J., & Samama, J. (1993). Crystal structure of Escherichia coli TEM1 β‐lactamase at 1.8 Å resolution. Proteins: Structure, Function, and Bioinformatics. https://doi.org/10.1002/prot.340160406
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