2g0b | pdb_00002g0b
The structure of FeeM, an N-acyl amino acid synthase from uncultured soil microbes
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| 2g0b, resolution 3.000Å | |||||||||||||
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| Ligands: | NLT | ||||||||||||
| Gene: | feem (uncultured bacterium) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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.
About this Structure
2G0B is a Single protein structure of sequence from Uncultured bacterium. Full crystallographic information is available from OCA.
Reference
FeeM, an N-acyl amino acid synthase from an uncultured soil microbe: structure, mechanism, and acyl carrier protein binding., Van Wagoner RM, Clardy J, Structure. 2006 Sep;14(9):1425-35. PMID:16962973
Page seeded by OCA on Thu Mar 20 16:58:53 2008
