An evolutionary classification of the metallo-beta-lactamase fold proteins - PubMed (original) (raw)
Affiliations
- PMID: 11471246
An evolutionary classification of the metallo-beta-lactamase fold proteins
L Aravind. In Silico Biol. 1999.
Abstract
All the detectable metallo-beta-lactamase fold proteins were identified in the publicly available sequence databases and complete genome sequences using iterative profile searches with the PSI-BLAST program and motif searches with position specific weight matrices. The catalytic site/mechanism and the corresponding structural elements were characterized for these proteins based on the available structure of the Bacillus zinc-dependent beta-lactamase. Based on pair-wise sequence and phylogenetic analysis an evolutionary classification for enzymes of this fold was developed and discussed in terms of implications for substrate specificity. Finally, some predicted inactive members which have been recruited for non-enzymatic functions such as microtubule binding in a cytoskeletal MAP1 are described.
Similar articles
- Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches.
Aravind L, Koonin EV. Aravind L, et al. J Mol Biol. 1999 Apr 16;287(5):1023-40. doi: 10.1006/jmbi.1999.2653. J Mol Biol. 1999. PMID: 10222208 - Metallo-beta-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily.
Bebrone C. Bebrone C. Biochem Pharmacol. 2007 Dec 15;74(12):1686-701. doi: 10.1016/j.bcp.2007.05.021. Epub 2007 Jun 2. Biochem Pharmacol. 2007. PMID: 17597585 Review. - Structural effects of the active site mutation cysteine to serine in Bacillus cereus zinc-beta-lactamase.
Chantalat L, Duée E, Galleni M, Frère JM, Dideberg O. Chantalat L, et al. Protein Sci. 2000 Jul;9(7):1402-6. doi: 10.1110/ps.9.7.1402. Protein Sci. 2000. PMID: 10933508 Free PMC article. - Effect of pH on the active site of an Arg121Cys mutant of the metallo-beta-lactamase from Bacillus cereus: implications for the enzyme mechanism.
Davies AM, Rasia RM, Vila AJ, Sutton BJ, Fabiane SM. Davies AM, et al. Biochemistry. 2005 Mar 29;44(12):4841-9. doi: 10.1021/bi047709t. Biochemistry. 2005. PMID: 15779910 - Outsmarting metallo-beta-lactamases by mimicking their natural evolution.
Oelschlaeger P. Oelschlaeger P. J Inorg Biochem. 2008 Dec;102(12):2043-51. doi: 10.1016/j.jinorgbio.2008.05.007. Epub 2008 May 28. J Inorg Biochem. 2008. PMID: 18602162 Review.
Cited by
- Modulation of diverse biological processes by CPSF, the master regulator of mRNA 3' ends.
Liu L, Manley JL. Liu L, et al. RNA. 2024 Aug 16;30(9):1122-1140. doi: 10.1261/rna.080108.124. RNA. 2024. PMID: 38986572 Free PMC article. Review. - Metallo-Beta-Lactamase-like Encoding Genes in Candidate Phyla Radiation: Widespread and Highly Divergent Proteins with Potential Multifunctionality.
Maatouk M, Merhej V, Pontarotti P, Ibrahim A, Rolain JM, Bittar F. Maatouk M, et al. Microorganisms. 2023 Jul 28;11(8):1933. doi: 10.3390/microorganisms11081933. Microorganisms. 2023. PMID: 37630493 Free PMC article. - Origin, Diversity, and Multiple Roles of Enzymes with Metallo-β-Lactamase Fold from Different Organisms.
Diene SM, Pontarotti P, Azza S, Armstrong N, Pinault L, Chabrière E, Colson P, Rolain JM, Raoult D. Diene SM, et al. Cells. 2023 Jun 30;12(13):1752. doi: 10.3390/cells12131752. Cells. 2023. PMID: 37443786 Free PMC article. Review. - Structure and Function of SNM1 Family Nucleases.
Wu HY, Zheng Y, Laciak AR, Huang NN, Koszelak-Rosenblum M, Flint AJ, Carr G, Zhu G. Wu HY, et al. Adv Exp Med Biol. 2023;1414:1-26. doi: 10.1007/5584_2022_724. Adv Exp Med Biol. 2023. PMID: 35708844 Review. - Dual targeting of Saccharomyces cerevisiae Pso2 to mitochondria and the nucleus, and its functional relevance in the repair of DNA interstrand crosslinks.
Somashekara SC, Muniyappa K. Somashekara SC, et al. G3 (Bethesda). 2022 May 30;12(6):jkac066. doi: 10.1093/g3journal/jkac066. G3 (Bethesda). 2022. PMID: 35482533 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials