Protein-protein interface analysis of the non-ribosomal peptide synthetase peptidyl carrier protein and enzymatic domains.
| Autor: | Corpuz JC; Department of Chemistry and Biochemistry, University of California-San Diego, 9500 Gilman Drive, La Jolla, CA, 92093-0358, USA., Sanlley JO; Department of Chemistry and Biochemistry, University of California-San Diego, 9500 Gilman Drive, La Jolla, CA, 92093-0358, USA., Burkart MD; Department of Chemistry and Biochemistry, University of California-San Diego, 9500 Gilman Drive, La Jolla, CA, 92093-0358, USA. |
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| Jazyk: | angličtina |
| Zdroj: | Synthetic and systems biotechnology [Synth Syst Biotechnol] 2022 Feb 16; Vol. 7 (2), pp. 677-688. Date of Electronic Publication: 2022 Feb 16 (Print Publication: 2022). |
| DOI: | 10.1016/j.synbio.2022.02.006 |
| Abstrakt: | Non-ribosomal peptide synthetases (NRPSs) are attractive targets for biosynthetic pathway engineering due to their modular architecture and the therapeutic relevance of their products. With catalysis mediated by specific protein-protein interactions formed between the peptidyl carrier protein (PCP) and its partner enzymes, NRPS enzymology and control remains fertile ground for discovery. This review focuses on the recent efforts within structural biology by compiling high-resolution structural data that shed light into the various protein-protein interfaces formed between the PCP and its partner enzymes, including the phosphopantetheinyl transferase (PPTase), adenylation (A) domain, condensation (C) domain, thioesterase (TE) domain and other tailoring enzymes within the synthetase. Integrating our understanding of how the PCP recognizes partner proteins with the potential to use directed evolution and combinatorial biosynthetic methods will enhance future efforts in discovery and production of new bioactive compounds. Competing Interests: We have no conflict of interest to declare. (© 2022 The Authors.) |
| Databáze: | MEDLINE |
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