Bacterial TEM-type serine beta-lactamases: structure and analysis of mutations

   


1. Chemical Department of M.V.Lomonosov Moscow State University, Moscow, Russia
2. Chemical Department of M.V.Lomonosov Moscow State University, Moscow, Russia; Center for Data-Intensive Biomedicine and Biotechnology, Skolkovo Institute of Science and Technology, Moscow, Russia
3. Institute of Physiologically Active Compounds, Moscow region, Chernogolovka, Russia
Type: Bioinformatics/Proteomics
DOI: 10.18097/PBMC20176306499      PubMed Id: 29251610
Year: 2017 vol: 63  issue:6  pages: 499-507
Abstract: Beta-lactamases (EC 3.5.2.6) represent a superfamily containing more than 2,000 members: it includes genetically and functionally different bacterial enzymes capable to destroy the beta-lactam antibiotics. The most common are beta-lactamases of molecular class A with serine in the active center. Among them, TEM-type beta-lactamases are of particular interest from the viewpoint of studying the mechanisms of the evolution of resistance 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 have been presented in Protein Data Bank. We have considered the main structural features of the enzymes of this type with particular attention to the analysis of key drug resistance and the secondary mutations, their location relative to the active center and the surface of the protein globule. We have developed the BlaSIDB database (www.blasidb.org) which is an open information resource combining available data on 3D structures, amino acid sequences and nomenclature of the corresponding forms of beta-lactamases.
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Reference: Grigorenko V.G., Rubtsova M.Yu., Uporov I.V., Ishtubaev I.V., Andreeva I.P., Shcherbinin D.S., Veselovsky A.V., Egorov A.M., Bacterial TEM-type serine beta-lactamases: structure and analysis of mutations, Biomeditsinskaya khimiya, 2017, vol: 63(6), 499-507.
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