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==Crystal structure of selenomethionine-labeled Thermus thermophilus FakA ATP-binding domain== | ==Crystal structure of selenomethionine-labeled Thermus thermophilus FakA ATP-binding domain== | ||
<StructureSection load='7ed9' size='340' side='right'caption='[[7ed9]]' scene=''> | <StructureSection load='7ed9' size='340' side='right'caption='[[7ed9]], [[Resolution|resolution]] 2.02Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ED9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ED9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7ed9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ED9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ED9 FirstGlance]. <br> | ||
</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=7ed9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ed9 OCA], [https://pdbe.org/7ed9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ed9 RCSB], [https://www.ebi.ac.uk/pdbsum/7ed9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ed9 ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7ed9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ed9 OCA], [https://pdbe.org/7ed9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ed9 RCSB], [https://www.ebi.ac.uk/pdbsum/7ed9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ed9 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5SLS9_THET8 Q5SLS9_THET8] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Fatty acid kinase is necessary for the incorporation of exogenous fatty acids into membrane phospholipids. Fatty acid kinase consists of two components: a kinase component, FakA, that phosphorylates a fatty acid bound to a fatty acid-binding component, FakB. However, the molecular details underlying the phosphotransfer reaction remain to be resolved. We determined the crystal structure of the N-terminal domain of FakA bound to ADP from Thermus thermophilus HB8. The overall structure of this domain showed that the helical barrel fold is similar to the nucleotide-binding component of dihydroxyacetone kinase. The structure of the nucleotide-binding site revealed the roles of the conserved residues in recognition of ADP and Mg(2+), but the N-terminal domain of FakA lacked the ADP-capping loop found in the dihydroxyacetone kinase component. Based on the structural similarity to the two subunits of dihydroxyacetone kinase complex, we constructed a model of the complex of T. thermophilus FakB and the N-terminal domain of FakA. In this model, the invariant Arg residue of FakB occupied a position that was spatially similar to that of the catalytically important Arg residue of dihydroxyacetone kinase, which predicted a composite active site in the Fatty acid kinase complex. | |||
Crystal structure of a nucleotide-binding domain of fatty acid kinase FakA from Thermus thermophilus HB8.,Nakatani M, Nakahara SY, Fukui K, Urano M, Fujii Y, Murakawa T, Baba S, Kumasaka T, Okanishi H, Kanai Y, Yano T, Masui R J Struct Biol. 2022 Dec;214(4):107904. doi: 10.1016/j.jsb.2022.107904. Epub 2022 , Oct 11. PMID:36228973<ref>PMID:36228973</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7ed9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Thermus thermophilus HB8]] | |||
[[Category: Fukui K]] | [[Category: Fukui K]] | ||
[[Category: Masui R]] | [[Category: Masui R]] | ||
Revision as of 10:44, 11 January 2023
Crystal structure of selenomethionine-labeled Thermus thermophilus FakA ATP-binding domainCrystal structure of selenomethionine-labeled Thermus thermophilus FakA ATP-binding domain
Structural highlights
FunctionPublication Abstract from PubMedFatty acid kinase is necessary for the incorporation of exogenous fatty acids into membrane phospholipids. Fatty acid kinase consists of two components: a kinase component, FakA, that phosphorylates a fatty acid bound to a fatty acid-binding component, FakB. However, the molecular details underlying the phosphotransfer reaction remain to be resolved. We determined the crystal structure of the N-terminal domain of FakA bound to ADP from Thermus thermophilus HB8. The overall structure of this domain showed that the helical barrel fold is similar to the nucleotide-binding component of dihydroxyacetone kinase. The structure of the nucleotide-binding site revealed the roles of the conserved residues in recognition of ADP and Mg(2+), but the N-terminal domain of FakA lacked the ADP-capping loop found in the dihydroxyacetone kinase component. Based on the structural similarity to the two subunits of dihydroxyacetone kinase complex, we constructed a model of the complex of T. thermophilus FakB and the N-terminal domain of FakA. In this model, the invariant Arg residue of FakB occupied a position that was spatially similar to that of the catalytically important Arg residue of dihydroxyacetone kinase, which predicted a composite active site in the Fatty acid kinase complex. Crystal structure of a nucleotide-binding domain of fatty acid kinase FakA from Thermus thermophilus HB8.,Nakatani M, Nakahara SY, Fukui K, Urano M, Fujii Y, Murakawa T, Baba S, Kumasaka T, Okanishi H, Kanai Y, Yano T, Masui R J Struct Biol. 2022 Dec;214(4):107904. doi: 10.1016/j.jsb.2022.107904. Epub 2022 , Oct 11. PMID:36228973[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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