2G0B
The structure of FeeM, an N-acyl amino acid synthase from uncultured soil microbes
Summary for 2G0B
| Entry DOI | 10.2210/pdb2g0b/pdb |
| Descriptor | FeeM, N-DODECANOYL-L-TYROSINE (3 entities in total) |
| Functional Keywords | n-acyl transferase, environmental dna, protein-product complex, antibiotic synthase, transferase |
| Biological source | uncultured bacterium |
| Total number of polymer chains | 8 |
| Total formula weight | 177153.70 |
| Authors | Van Wagoner, R.M.,Clardy, J. (deposition date: 2006-02-11, release date: 2006-09-26, Last modification date: 2024-02-14) |
| Primary citation | 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 Cited by 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: 16962973DOI: 10.1016/j.str.2006.07.005 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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