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| | ==Structure of FabK from Thermotoga maritima== | | ==Structure of FabK from Thermotoga maritima== |
| - | <StructureSection load='5gvh' size='340' side='right' caption='[[5gvh]], [[Resolution|resolution]] 2.29Å' scene=''> | + | <StructureSection load='5gvh' size='340' side='right'caption='[[5gvh]], [[Resolution|resolution]] 2.29Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5gvh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GVH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GVH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5gvh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GVH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GVH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.294Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gvj|5gvj]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM_0800, Tmari_0801 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</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=5gvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gvh OCA], [https://pdbe.org/5gvh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gvh RCSB], [https://www.ebi.ac.uk/pdbsum/5gvh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gvh ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5gvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gvh OCA], [http://pdbe.org/5gvh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gvh RCSB], [http://www.ebi.ac.uk/pdbsum/5gvh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gvh ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/R4NR95_THEMA R4NR95_THEMA] |
| | <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 5gvh" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5gvh" 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: Thema]] | + | [[Category: Large Structures]] |
| - | [[Category: Ha, B H]] | + | [[Category: Thermotoga maritima MSB8]] |
| - | [[Category: Kim, E E]] | + | [[Category: Ha BH]] |
| - | [[Category: Moon, J H]] | + | [[Category: Kim EE]] |
| - | [[Category: Shin, S C]] | + | [[Category: Moon JH]] |
| - | [[Category: Enoyl-acp reductase ii]] | + | [[Category: Shin SC]] |
| - | [[Category: Fabk]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
R4NR95_THEMA
Publication Abstract from PubMed
TM0800 from Thermotoga maritima is one of the hypothetical proteins with unknown function. The crystal structure determined at 2.3 A resolution reveals a two domain structure: the N-terminal domain forming a barrel and the C-terminal forming a lid. One FMN is bound between the two domains with the phosphate making intricate hydrogen bonds with protein and three tightly bound water molecules, and the isoalloxazine ring packed against the side chains of Met22 and Met276. The structure is almost identical to that of FabK (enoyl-acyl carrier protein (ACP) reductase, ENR II), a key enzyme in bacterial type II fatty-acid biosynthesis that catalyzes the final step in each elongation cycle; and the enzymatic activity confirms that TM0800 is an ENR. Enzymatic activity was almost completely abolished when the helices connecting the barrel and the lid were deleted. Also, the Met276Ala and Ser280Ala mutants showed a significant reduction in enzymatic activity. The crystal structure of Met276Ala mutant at 1.9 A resolution showed an absence of FMN suggesting that FMN plays a role in catalysis, and Met276 is important in positioning FMN. TmFabK exists as a dimer in both solution and crystal. Together this study provides molecular basis for the catalytic activity of FabK.
Structural and biochemical characterization of FabK from Thermotoga maritima.,Ha BH, Shin SC, Moon JH, Keum G, Kim CW, Kim EE Biochem Biophys Res Commun. 2017 Jan 22;482(4):968-974. doi:, 10.1016/j.bbrc.2016.11.141. Epub 2016 Nov 28. PMID:27908729[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ha BH, Shin SC, Moon JH, Keum G, Kim CW, Kim EE. Structural and biochemical characterization of FabK from Thermotoga maritima. Biochem Biophys Res Commun. 2017 Jan 22;482(4):968-974. doi:, 10.1016/j.bbrc.2016.11.141. Epub 2016 Nov 28. PMID:27908729 doi:http://dx.doi.org/10.1016/j.bbrc.2016.11.141
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