6kia

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Current revision (10:42, 27 March 2024) (edit) (undo)
 
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<StructureSection load='6kia' size='340' side='right'caption='[[6kia]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='6kia' size='340' side='right'caption='[[6kia]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6kia]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Uncultivated_bacterium Uncultivated bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KIA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6KIA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6kia]] is a 3 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=6KIA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KIA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5979826&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6kia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kia OCA], [http://pdbe.org/6kia PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kia RCSB], [http://www.ebi.ac.uk/pdbsum/6kia PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kia ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6kia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kia OCA], [https://pdbe.org/6kia PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kia RCSB], [https://www.ebi.ac.uk/pdbsum/6kia PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kia ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A1C9HA64_9BACT A0A1C9HA64_9BACT]
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The synthetic biocide triclosan targets enoyl-acyl carrier protein reductase(s) (ENR) in bacterial type II fatty acid biosynthesis. Screening and sequence analyses of the triclosan resistome from the soil metagenome identified a variety of triclosan-resistance ENRs. Interestingly, the mode of triclosan resistance by one hypothetical protein was elusive, mainly due to a lack of sequence similarity with other proteins that mediate triclosan resistance. Here, we carried out a structure-based function prediction of the hypothetical protein, herein referred to as FabMG, and in vivo and in vitro functional analyses. The crystal structure of FabMG showed limited structural homology with FabG and FabI, which are also involved in type II fatty acid synthesis. In vivo complementation and in vitro activity assays indicated that FabMG is functionally a FabI-type ENR that employs NADH as a coenzyme. Variations in the sequence and structure of FabMG are likely responsible for inefficient binding of triclosan, resulting in triclosan resistance. These data unravel a previously uncharacterized FabMG, which is prevalent in various microbes in triclosan-contaminated environments and provide mechanistic insight into triclosan resistance.
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A triclosan-resistance protein from the soil metagenome is a novel enoyl-acyl carrier protein reductase: Structure-guided functional analysis.,Kim SH, Khan R, Choi K, Lee SW, Rhee S FEBS J. 2020 Feb 28. doi: 10.1111/febs.15267. PMID:32112503<ref>PMID:32112503</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6kia" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Enoyl-Acyl-Carrier Protein Reductase 3D structures|Enoyl-Acyl-Carrier Protein Reductase 3D structures]]
*[[Enoyl-Acyl-Carrier Protein Reductase 3D structures|Enoyl-Acyl-Carrier Protein Reductase 3D structures]]
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== References ==
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*[[Tyrosine kinase 3D structures|Tyrosine kinase 3D structures]]
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Uncultivated bacterium]]
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[[Category: Uncultured bacterium]]
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[[Category: Kim, S]]
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[[Category: Kim S]]
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[[Category: Rhee, S]]
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[[Category: Rhee S]]
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[[Category: Enoyl-acyl carrier protein reductase]]
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[[Category: Fabmg]]
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[[Category: Oxidoreductase]]
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Current revision

NADH bound structure of FabMG, novel type of Enoyl-acyl carrier protein reductase

PDB ID 6kia

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