2g0b
From Proteopedia
(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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==Overview== | ==Overview== | ||
| - | Attempts to access antibiotics by capturing biosynthetic genes and | + | 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== | ==About this Structure== | ||
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[[Category: Uncultured bacterium]] | [[Category: Uncultured bacterium]] | ||
[[Category: Clardy, J.]] | [[Category: Clardy, J.]] | ||
| - | [[Category: Wagoner, R | + | [[Category: Wagoner, R M.Van.]] |
[[Category: NLT]] | [[Category: NLT]] | ||
[[Category: antibiotic synthase]] | [[Category: antibiotic synthase]] | ||
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[[Category: protein-product complex]] | [[Category: protein-product complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:26:54 2008'' |
Revision as of 15:26, 21 February 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
Page seeded by OCA on Thu Feb 21 17:26:54 2008
