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The PASTA domain: a beta-lactam-binding domain.
Corin Yeats1, Robert D Finn, Alex Bateman
1The Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge, UK CB10 1SA. cay@sanger.ac.uk
Trends in Biochemical Sciences
|September 10, 2002
Summary
The newly identified PASTA domain, found in pathogen kinases and penicillin-binding proteins, likely binds beta-lactam antibiotics. This suggests a novel mechanism for how these crucial drugs combat infections.
Area of Science:
- Microbiology
- Biochemistry
- Drug Discovery
Background:
- The PASTA domain is present in high molecular weight penicillin-binding proteins and serine/threonine kinases in various pathogens.
- These proteins are essential in microbial pathogens.
Purpose of the Study:
- To characterize the previously unexamined PASTA domain.
- To investigate the functional role of the PASTA domain in pathogen biology and antibiotic interaction.
Main Methods:
- Bioinformatic analysis to identify the PASTA domain across different species.
- Inference of biochemical function based on domain structure and known protein interactions.
Main Results:
- The PASTA domain is described and identified in key pathogen proteins.
- It is inferred that the PASTA domain binds beta-lactam antibiotics and peptidoglycan analogues.
- PknB-like kinases containing the PASTA domain are proposed as critical regulators of cell-wall biosynthesis.
Conclusions:
- The PASTA domain represents a novel target for beta-lactam antibiotic interaction.
- These findings suggest an additional mechanism of action for beta-lactam antibiotics in combating pathogens.
- Understanding the PASTA domain's role could lead to new therapeutic strategies.