6lkh
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==Two-component system protein mediate signal transduction== |
| - | <StructureSection load='6lkh' size='340' side='right'caption='[[6lkh]]' scene=''> | + | <StructureSection load='6lkh' size='340' side='right'caption='[[6lkh]], [[Resolution|resolution]] 2.53Å' 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= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6lkh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus] and [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_NCTC_8325 Staphylococcus aureus subsp. aureus NCTC 8325]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LKH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LKH 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=6lkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lkh OCA], [https://pdbe.org/6lkh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lkh RCSB], [https://www.ebi.ac.uk/pdbsum/6lkh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lkh ProSAT]</span></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]] 2.534Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</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=6lkh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lkh OCA], [https://pdbe.org/6lkh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lkh RCSB], [https://www.ebi.ac.uk/pdbsum/6lkh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lkh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/X5DVD1_STAAU X5DVD1_STAAU] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Two-component systems (TCS), which typically consist of a membrane-embedded histidine kinase and a cytoplasmic response regulator, are the dominant signaling proteins for transduction of environmental stimuli into cellular response pathways in prokaryotic cells. HptRSA is a recently identified TCS consisting of the G6P-associated sensor protein (HptA), transmembrane histidine kinase (HptS), and cytoplasmic effector (HptR). HptRSA mediates glucose-6-phosphate (G6P) uptake to support Staphylococcus aureus growth and multiplication within various host cells. How the mechanism by which HptRSA perceives G6P and triggers a downstream response has remained elusive. Here, we solved the HptA structures in apo and G6P-bound states. G6P binding in the cleft between two HptA domains caused a conformational closing movement. The solved structures of HptA in complex with the periplasmic domain of HptS showed that HptA interacts with HptS through both constitutive and switchable interfaces. The G6P-free form of HptA binds to the membrane-distal side of the HptS periplasmic domain (HptSp), resulting in a parallel conformation of the HptSp protomer pair. However, once HptA associates with G6P, its intramolecular domain closure switches the HptA-HptSp contact region into the membrane-proximal domain, which causes rotation and closure of the C termini of each HptSp protomer. Through biochemical and growth assays of HptA and HptS mutant variants, we proposed a distinct mechanism of interface switch-mediated signaling transduction. Our results provide mechanistic insights into bacterial nutrient sensing and expand our understanding of the activation modes by which TCS communicates external signals. | ||
| + | |||
| + | Interface switch mediates signal transmission in a two-component system.,Wang M, Guo Q, Zhu K, Fang B, Yang Y, Teng M, Li X, Tao Y Proc Natl Acad Sci U S A. 2020 Dec 1;117(48):30433-30440. doi:, 10.1073/pnas.1912080117. Epub 2020 Nov 16. PMID:33199635<ref>PMID:33199635</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6lkh" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Staphylococcus aureus]] |
| + | [[Category: Staphylococcus aureus subsp. aureus NCTC 8325]] | ||
| + | [[Category: Tao Y]] | ||
| + | [[Category: Wang M]] | ||
Current revision
Two-component system protein mediate signal transduction
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