2g0b
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= feem ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=77133 uncultured bacterium]) | |GENE= feem ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=77133 uncultured bacterium]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2g0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g0b OCA], [http://www.ebi.ac.uk/pdbsum/2g0b PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2g0b RCSB]</span> | ||
}} | }} | ||
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[[Category: Clardy, J.]] | [[Category: Clardy, J.]] | ||
[[Category: Wagoner, R M.Van.]] | [[Category: Wagoner, R M.Van.]] | ||
| - | [[Category: NLT]] | ||
[[Category: antibiotic synthase]] | [[Category: antibiotic synthase]] | ||
[[Category: environmental dna]] | [[Category: environmental dna]] | ||
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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 Mon Mar 31 03:10:09 2008'' |
Revision as of 00:10, 31 March 2008
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| , resolution 3.000Å | |||||||
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| Ligands: | |||||||
| Gene: | feem (uncultured bacterium) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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