7w7h: Difference between revisions
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==S Suis FakA-FakB2 complex structure== | |||
<StructureSection load='7w7h' size='340' side='right'caption='[[7w7h]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7w7h]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_suis_05ZYH33 Streptococcus suis 05ZYH33]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7W7H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7W7H FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7w7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7w7h OCA], [https://pdbe.org/7w7h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7w7h RCSB], [https://www.ebi.ac.uk/pdbsum/7w7h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7w7h ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A4VXI8_STRSY A4VXI8_STRSY] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Staphylococcus and Streptococcus, two groups of major human pathogens, are equipped with a fatty acid kinase (Fak) machinery to scavenge host fatty acids. The Fak complex is contains an ATP-binding subunit FakA, which interacts with varied FakB isoforms, and synthesizes acyl-phosphate from extracellular fatty acids. However, how FakA recognizes its FakB partners and then activates different fatty acids is poorly understood. Here, we systematically describe the Fak system from the zoonotic pathogen, Streptococcus suis. The crystal structure of SsFakA complexed with SsFakB2 was determined at 2.6 A resolution. An in vitro system of Fak-PlsX (phosphate: acyl-ACP transacylase) was developed to track acyl-phosphate intermediate and its final product acyl-ACP. Structure-guided mutagenesis enabled us to characterize a mechanism for streptococcal FakA working with FakB partners engaged in host fatty acid scavenging. These findings offer a comprehensive description of the Fak kinase machinery, thus advancing the discovery of attractive targets against deadly infections with Streptococcus. | |||
Structure and mechanism for streptococcal fatty acid kinase (Fak) system dedicated to host fatty acid scavenging.,Shi Y, Zang N, Lou N, Xu Y, Sun J, Huang M, Zhang H, Lu H, Zhou C, Feng Y Sci Adv. 2022 Sep 2;8(35):eabq3944. doi: 10.1126/sciadv.abq3944. Epub 2022 Sep 2. PMID:36054360<ref>PMID:36054360</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7w7h" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptococcus suis 05ZYH33]] | |||
[[Category: Feng Y]] | |||
[[Category: Huang M]] | |||
[[Category: Lou N]] | |||
[[Category: Lu H]] | |||
[[Category: Shi Y]] | |||
[[Category: Sun J]] | |||
[[Category: Xu Y]] | |||
[[Category: Zang N]] | |||
[[Category: Zhang H]] | |||
[[Category: Zhou C]] | |||
Latest revision as of 20:37, 29 November 2023
S Suis FakA-FakB2 complex structureS Suis FakA-FakB2 complex structure
Structural highlights
FunctionPublication Abstract from PubMedStaphylococcus and Streptococcus, two groups of major human pathogens, are equipped with a fatty acid kinase (Fak) machinery to scavenge host fatty acids. The Fak complex is contains an ATP-binding subunit FakA, which interacts with varied FakB isoforms, and synthesizes acyl-phosphate from extracellular fatty acids. However, how FakA recognizes its FakB partners and then activates different fatty acids is poorly understood. Here, we systematically describe the Fak system from the zoonotic pathogen, Streptococcus suis. The crystal structure of SsFakA complexed with SsFakB2 was determined at 2.6 A resolution. An in vitro system of Fak-PlsX (phosphate: acyl-ACP transacylase) was developed to track acyl-phosphate intermediate and its final product acyl-ACP. Structure-guided mutagenesis enabled us to characterize a mechanism for streptococcal FakA working with FakB partners engaged in host fatty acid scavenging. These findings offer a comprehensive description of the Fak kinase machinery, thus advancing the discovery of attractive targets against deadly infections with Streptococcus. Structure and mechanism for streptococcal fatty acid kinase (Fak) system dedicated to host fatty acid scavenging.,Shi Y, Zang N, Lou N, Xu Y, Sun J, Huang M, Zhang H, Lu H, Zhou C, Feng Y Sci Adv. 2022 Sep 2;8(35):eabq3944. doi: 10.1126/sciadv.abq3944. Epub 2022 Sep 2. PMID:36054360[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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