7ed6: Difference between revisions

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<StructureSection load='7ed6' size='340' side='right'caption='[[7ed6]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
<StructureSection load='7ed6' size='340' side='right'caption='[[7ed6]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7ed6]] 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=7ED6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ED6 FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ED6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ED6 FirstGlance]. <br>
</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>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 1.9285033&#8491;</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>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=7ed6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ed6 OCA], [https://pdbe.org/7ed6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ed6 RCSB], [https://www.ebi.ac.uk/pdbsum/7ed6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ed6 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=7ed6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ed6 OCA], [https://pdbe.org/7ed6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ed6 RCSB], [https://www.ebi.ac.uk/pdbsum/7ed6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ed6 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7ed6" 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]]

Latest revision as of 16:33, 6 November 2024

Crystal structure of Thermus thermophilus FakA ATP-binding domainCrystal structure of Thermus thermophilus FakA ATP-binding domain

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9285033Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

7ed6, resolution 1.93Å

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OCA
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