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| | <StructureSection load='6vly' size='340' side='right'caption='[[6vly]], [[Resolution|resolution]] 1.86Å' scene=''> | | <StructureSection load='6vly' size='340' side='right'caption='[[6vly]], [[Resolution|resolution]] 1.86Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6vly]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ahn_2437 Ahn 2437]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VLY OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VLY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6vly]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Alistipes_finegoldii Alistipes finegoldii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6VLY FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</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]] 1.86Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabI, ERS852447_01935 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=214856 AHN 2437])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Enoyl-[acyl-carrier-protein]_reductase_(NADH) Enoyl-[acyl-carrier-protein] reductase (NADH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.9 1.3.1.9] </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=6vly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vly OCA], [https://pdbe.org/6vly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vly RCSB], [https://www.ebi.ac.uk/pdbsum/6vly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vly ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vly OCA], [http://pdbe.org/6vly PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vly RCSB], [http://www.ebi.ac.uk/pdbsum/6vly PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vly ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A174E195_9BACT A0A174E195_9BACT] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6vly" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6vly" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Enoyl-Acyl-Carrier Protein Reductase 3D structures|Enoyl-Acyl-Carrier Protein Reductase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ahn 2437]] | + | [[Category: Alistipes finegoldii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Radka, C D]] | + | [[Category: Radka CD]] |
| - | [[Category: Rock, C O]] | + | [[Category: Rock CO]] |
| - | [[Category: Seetharaman, J]] | + | [[Category: Seetharaman J]] |
| - | [[Category: Enoyl-acp reductase]]
| + | |
| - | [[Category: Fabi]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
A0A174E195_9BACT
Publication Abstract from PubMed
Enoyl-acyl carrier protein reductase (FabI) catalyzes a rate-controlling step in bacterial fatty-acid synthesis and is a target for antibacterial drug development. A phylogenetic analysis shows that FabIs fall into four divergent clades. Members of clades 1-3 have been structurally and biochemically characterized, but the fourth clade found in members of phylum Bacteroidetes is uncharacterized. Here, we identified the unique structure and conformational changes that distinguish clade 4 FabIs. Alistipes finegoldii is a prototypical Bacteroidetes inhabitant of the gut microbiome. We found that A. finegoldii FabI (AfFabI) displays cooperative kinetics and uses NADH as a cofactor, and its crystal structure at 1.72 A resolution showed that it adopts a Rossmann fold as do other characterized FabIs. It also disclosed a C-terminal extension that forms a helix-helix interaction that links the protomers as a unique feature of AfFabI. An AfFabI*NADH crystal structure at 1.86 A resolution revealed that this feature undergoes a large conformational change to participate in covering the NADH-binding pocket and establishing the water channels that connect the active site to the central water well. Progressive deletion of these interactions led to catalytically compromised proteins that fail to bind NADH. This unique conformational change imparted a distinct shape to the AfFabI active site that renders it refractory to a FabI drug that targets clade 1 and 3 pathogens. We conclude that the clade 4 FabI, found in the Bacteroidetes inhabitants of the gut, have several structural features and conformational transitions that distinguish them from other bacterial FabIs.
The genome of a Bacteroidetes inhabitant of the human gut encodes a structurally distinct enoyl-acyl carrier protein reductase (FabI).,Radka CD, Frank MW, Yao J, Seetharaman J, Miller DJ, Rock CO J Biol Chem. 2020 Apr 21. pii: RA120.013336. doi: 10.1074/jbc.RA120.013336. PMID:32317282[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Radka CD, Frank MW, Yao J, Seetharaman J, Miller DJ, Rock CO. The genome of a Bacteroidetes inhabitant of the human gut encodes a structurally distinct enoyl-acyl carrier protein reductase (FabI). J Biol Chem. 2020 Apr 21. pii: RA120.013336. doi: 10.1074/jbc.RA120.013336. PMID:32317282 doi:http://dx.doi.org/10.1074/jbc.RA120.013336
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