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| | ==X-Ray Structure of Enoyl-Acyl Carrier Protein Reductase from Bacillus Anthracis with c-terminal His tag (Apo form)== | | ==X-Ray Structure of Enoyl-Acyl Carrier Protein Reductase from Bacillus Anthracis with c-terminal His tag (Apo form)== |
| - | <StructureSection load='5ycx' size='340' side='right' caption='[[5ycx]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='5ycx' size='340' side='right'caption='[[5ycx]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ycx]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YCX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YCX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ycx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_14579 Bacillus cereus ATCC 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YCX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YCX FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.701Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ycx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ycx OCA], [http://pdbe.org/5ycx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ycx RCSB], [http://www.ebi.ac.uk/pdbsum/5ycx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ycx 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=5ycx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ycx OCA], [https://pdbe.org/5ycx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ycx RCSB], [https://www.ebi.ac.uk/pdbsum/5ycx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ycx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FABI_BACCR FABI_BACCR]] Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). | + | [https://www.uniprot.org/uniprot/FABI_BACCR FABI_BACCR] Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity). |
| | <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 5ycx" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5ycx" 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: Kim, H T]] | + | [[Category: Bacillus cereus ATCC 14579]] |
| - | [[Category: Antibacterial]] | + | [[Category: Large Structures]] |
| - | [[Category: Fabi]] | + | [[Category: Kim HT]] |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
FABI_BACCR Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity).
Publication Abstract from PubMed
Enoyl-ACP reductase (ENR, also known as FabI) has received considerable interest as an anti-bacterial target due to its essentiality in fatty acid synthesis. All the FabI structures reported to date, regardless of the organism, are composed of homo-tetramers, except for two structures: Bacillus cereus and Staphylococcus aureus FabI (bcFabI and saFabI, respectively), which have been reported as dimers. However, the reason for the existence of the dimeric form in these organisms and the biological meaning of dimeric and tetrameric forms of FabI are ambiguous. Herein, we report the high-resolution crystal structure of a dimeric form of Bacillus anthracis FabI (baFabI) and the crystal structures of tetrameric forms of baFabI in the apo state and in complex with NAD(+) and with NAD(+)-triclosan, at 1.7 A, 1.85 A, 1.96 A, and 1.95 A, respectively. Interestingly, we found that baFabI with a His6-tag at its C-terminus exists as a dimer, whereas untagged-baFabI exists as a tetramer. The His6-tag may block the dimer-tetramer transition, since baFabI has relatively short-length amino acids ((255)LG(256)) after the 310-helix eta7 compared to those of FabI of other organisms. The dimeric form of baFabI is catalytically inactive, because the alpha-helix alpha5 occupies the NADH-binding site. During the process of dimer-tetramer transition, this alpha5 helix rotates about 55 degrees toward the tetramer interface and the active site is established. Therefore, tetramerization of baFabI is required for cofactor binding and catalytic activity.
Structural insights into the dimer-tetramer transition of FabI from Bacillus anthracis.,Kim HT, Kim S, Na BK, Chung J, Hwang E, Hwang KY Biochem Biophys Res Commun. 2017 Nov 4;493(1):28-33. doi:, 10.1016/j.bbrc.2017.09.084. Epub 2017 Sep 19. PMID:28935372[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kim HT, Kim S, Na BK, Chung J, Hwang E, Hwang KY. Structural insights into the dimer-tetramer transition of FabI from Bacillus anthracis. Biochem Biophys Res Commun. 2017 Nov 4;493(1):28-33. doi:, 10.1016/j.bbrc.2017.09.084. Epub 2017 Sep 19. PMID:28935372 doi:http://dx.doi.org/10.1016/j.bbrc.2017.09.084
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