2g0b
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(New page: 200px<br /><applet load="2g0b" size="350" color="white" frame="true" align="right" spinBox="true" caption="2g0b, resolution 3.000Å" /> '''The structure of Fe...)
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Revision as of 17:48, 29 January 2008
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The structure of FeeM, an N-acyl amino acid synthase from uncultured soil microbes
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 with as ligand. 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
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