Structural and functional analyses of the tridomain-nonribosomal peptide synthetase FmoA3 for 4-methyloxazoline ring formation
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ABSTRACT:
SUBMITTER: Naruhiko Adachi
PROVIDER: EMPIAR-11059 | biostudies-other |
REPOSITORIES: biostudies-other
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Structural and Functional Analyses of the Tridomain-Nonribosomal Peptide Synthetase FmoA3 for 4-Methyloxazoline Ring Formation.
Katsuyama Yohei Y Sone Kaoru K Harada Ayaka A Kawai Seiji S Urano Naoki N Adachi Naruhiko N Moriya Toshio T Kawasaki Masato M Shin-Ya Kazuo K Senda Toshiya T Ohnishi Yasuo Y
Angewandte Chemie (International ed. in English) 20210517 26
Nonribosomal peptide synthetases (NRPSs) are attractive targets for bioengineering to generate useful peptides. FmoA3 is a single modular NRPS composed of heterocyclization (Cy), adenylation (A), and peptidyl carrier protein (PCP) domains. It uses α-methyl-l-serine to synthesize a 4-methyloxazoline ring, probably with another Cy domain in the preceding module FmoA2. Here, we determined the head-to-tail homodimeric structures of FmoA3 by X-ray crystallography (apo-form, with adenylyl-imidodiphosp ...[more]
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