2G0B

The structure of FeeM, an N-acyl amino acid synthase from uncultured soil microbes

2G0B の概要

• エントリーDOI: 10.2210/pdb2g0b/pdb
• 分子名称: FeeM, N-DODECANOYL-L-TYROSINE (3 entities in total)
• 機能のキーワード: n-acyl transferase, environmental dna, protein-product complex, antibiotic synthase, transferase
• 由来する生物種: uncultured bacterium
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 177153.70

構造登録者

Van Wagoner, R.M.,Clardy, J. (登録日: 2006-02-11, 公開日: 2006-09-26, 最終更新日: 2024-02-14)

主引用文献

Van Wagoner, R.M.,Clardy, J.
FeeM, an N-Acyl Amino Acid Synthase from an Uncultured Soil Microbe: Structure, Mechanism, and Acyl Carrier Protein Binding.
Structure, 14:1425-1435, 2006

PubMed Abstract: Attempts to access antibiotics by capturing biosynthetic genes and pathways directly from environmental DNA, which is overwhelmingly derived from uncultured bacteria, have revealed a large and previously unknown family of N-acyl amino acid synthases (NASs). The structure of the NAS FeeM reveals structural similarity to the GCN5-related N-acyl transferases and acylhomoserine lactone synthases. The overall structure has a central beta sheet with alpha helices on both sides. A bound product at a cleft in the beta sheet identifies the active site and the structural basis for catalysis, and sequence conservation in this region indicates a bias for recognition over speed. FeeM interacts with an acyl carrier protein (FeeL), and the structure, mutagenesis, and enzymatic measurements reveal that a small hydrophobic pocket in alpha helix 5 dominates binding of FeeM to FeeL. The structural and mechanistic analyses suggest that the products of FeeM could be bacterial signaling agents.

PubMed: 16962973
DOI: 10.1016/j.str.2006.07.005

実験手法

X-RAY DIFFRACTION (3 Å)