4x9x
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4x9x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_MW2 Staphylococcus aureus subsp. aureus MW2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X9X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X9X FirstGlance]. <br> | <table><tr><td colspan='2'>[[4x9x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_MW2 Staphylococcus aureus subsp. aureus MW2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X9X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X9X FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</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]] 1.199Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=OLA:OLEIC+ACID'>OLA</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=4x9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x9x OCA], [https://pdbe.org/4x9x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x9x RCSB], [https://www.ebi.ac.uk/pdbsum/4x9x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x9x 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=4x9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x9x OCA], [https://pdbe.org/4x9x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x9x RCSB], [https://www.ebi.ac.uk/pdbsum/4x9x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x9x ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Y1315_STAAW Y1315_STAAW] May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism. | [https://www.uniprot.org/uniprot/Y1315_STAAW Y1315_STAAW] May bind long-chain fatty acids, such as palmitate, and may play a role in lipid transport or fatty acid metabolism. | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Fatty acid kinase (Fak) is a ubiquitous Gram-positive bacterial enzyme consisting of an ATP binding protein (FakA) that phosphorylates the fatty acid bound to FakB. In Staphylococcus aureus, Fak is a global regulator of virulence factor transcription and is essential for the activation of exogenous fatty acids for incorporation into phospholipids. The 1.2 A X-ray structure of S. aureus FakB2, activity assays, solution studies, site-directed mutagenesis and in vivo complementation were used to define the functions of the 5 conserved residues that define the FakB protein family (Pfam02645). The fatty acid tail is buried within the protein and the exposed carboxyl group is bound by a Ser93-fatty acid carboxyl-Thr61-His266 hydrogen bond network. The guanidinium of the invariant Arg170 is positioned to potentially interact with a bound acyl-phosphate. The reduced thermal denaturation temperatures of the T61A, S93A and H266A FakB2 mutants illustrate the importance of the hydrogen bond network in protein stability. The FakB2 T61A, S93A, and H266A mutants are 1000-fold less active in the Fak assay and the R170A mutant is completely inactive. All FakB2 mutants form FakA(FakB2)2 complexes except FakB2(R202A), which is deficient in FakA binding. Allelic replacement shows that strains expressing FakB2 mutants are defective in fatty acid incorporation into phospholipids and virulence gene transcription. These conserved residues are likely to perform the same critical functions in all bacterial fatty acid binding proteins. | ||
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| - | Biochemical roles for conserved residues in the bacterial fatty acid binding protein family.,Broussard TC, Miller DJ, Jackson P, Nourse A, White SW, Rock CO J Biol Chem. 2016 Jan 16. pii: jbc.M115.706820. PMID:26774272<ref>PMID:26774272</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4x9x" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Biochemical Roles for Conserved Residues in the Bacterial Fatty Acid Binding Protein Family
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