2g0b: Difference between revisions

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==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.

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==

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[[Category: Uncultured bacterium]]

[[Category: Clardy, J.]]

[[Category: Wagoner, R.M.Van.]]

[[Category: Wagoner, R M.Van.]]

[[Category: NLT]]

[[Category: antibiotic synthase]]

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[[Category: protein-product complex]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 14: / Line 14: @@
 [[Category: Uncultured bacterium]]
 [[Category: Clardy, J.]]
-[[Category: Wagoner, R.M.Van.]]
+[[Category: Wagoner, R M.Van.]]
 [[Category: NLT]]
 [[Category: antibiotic synthase]]
@@ Line 21: / Line 21: @@
 [[Category: protein-product complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:48:46 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:26:54 2008''