2g0b: Difference between revisions

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<StructureSection load='2g0b' size='340' side='right'caption='[[2g0b]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='2g0b' size='340' side='right'caption='[[2g0b]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2g0b]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultivated_bacterium Uncultivated bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G0B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G0B FirstGlance]. <br>
<table><tr><td colspan='2'>[[2g0b]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_bacterium Uncultured bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G0B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G0B FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NLT:N-DODECANOYL-L-TYROSINE'>NLT</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">feem ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=77133 uncultivated bacterium])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NLT:N-DODECANOYL-L-TYROSINE'>NLT</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2g0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g0b OCA], [https://pdbe.org/2g0b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g0b RCSB], [https://www.ebi.ac.uk/pdbsum/2g0b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g0b ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2g0b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g0b OCA], [https://pdbe.org/2g0b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g0b RCSB], [https://www.ebi.ac.uk/pdbsum/2g0b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g0b ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8KNZ7_9BACT Q8KNZ7_9BACT]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2g0b ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2g0b ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:16962973</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2g0b" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Uncultivated bacterium]]
[[Category: Uncultured bacterium]]
[[Category: Clardy, J]]
[[Category: Clardy J]]
[[Category: Wagoner, R M.Van]]
[[Category: Van Wagoner RM]]
[[Category: Antibiotic synthase]]
[[Category: Environmental dna]]
[[Category: N-acyl transferase]]
[[Category: Protein-product complex]]
[[Category: Transferase]]

Latest revision as of 09:26, 14 February 2024

The structure of FeeM, an N-acyl amino acid synthase from uncultured soil microbes

2g0b, resolution 3.00Å

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