Bacterial TEM-Type Serine Beta-Lactamases: Structure and Analysis of Mutations

Bacterial TEM-Type Serine Beta-Lactamases: Structure and Analysis of Mutations Beta-lactamases (EC 3.5.2.6) represent a superfamily containing more than 2000 members: it includes genetically and functionally different bacterial enzymes capable to degrade the beta-lactam antibiotics. Beta-lactamases of molecular class A with serine residue in the active center are the most common ones. In the context of studies of the mechanisms underlying of evolution of the resistance, TEM type beta-lactamases are of particular interest due to their broad polymorphism. To date, more than 200 sequences of TEM type beta-lactamases have been described and more than 60 structures of different mutant forms of these enzymes have been presented in the Protein Data Bank. We have considered here the main structural features of the enzymes of this type with particular attention to the analysis of key mutations determining drug resistance and the secondary mutations, their location relative to the active center and the surface of the protein globule. We have developed a BlaSIDB database (www.blasidb.org) which is an open information resource combining available data on 3D structures, amino acid sequences and nomenclature of the TEM type beta-lactamases. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biochemistry (Moscow) Supplement Series B: Biomedical Chemistry Springer Journals
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Publisher
Pleiades Publishing
Copyright
Copyright © 2018 by Pleiades Publishing, Ltd.
Subject
Chemistry; Bioorganic Chemistry; Medicinal Chemistry
ISSN
1990-7508
eISSN
1990-7516
D.O.I.
10.1134/S1990750818020038
Publisher site
See Article on Publisher Site

Abstract

Beta-lactamases (EC 3.5.2.6) represent a superfamily containing more than 2000 members: it includes genetically and functionally different bacterial enzymes capable to degrade the beta-lactam antibiotics. Beta-lactamases of molecular class A with serine residue in the active center are the most common ones. In the context of studies of the mechanisms underlying of evolution of the resistance, TEM type beta-lactamases are of particular interest due to their broad polymorphism. To date, more than 200 sequences of TEM type beta-lactamases have been described and more than 60 structures of different mutant forms of these enzymes have been presented in the Protein Data Bank. We have considered here the main structural features of the enzymes of this type with particular attention to the analysis of key mutations determining drug resistance and the secondary mutations, their location relative to the active center and the surface of the protein globule. We have developed a BlaSIDB database (www.blasidb.org) which is an open information resource combining available data on 3D structures, amino acid sequences and nomenclature of the TEM type beta-lactamases.

Journal

Biochemistry (Moscow) Supplement Series B: Biomedical ChemistrySpringer Journals

Published: May 30, 2018

References

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