3zx6: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3zx6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZX6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZX6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3zx6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZX6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZX6 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3zx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zx6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zx6 RCSB], [http://www.ebi.ac.uk/pdbsum/3zx6 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3zx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zx6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zx6 RCSB], [http://www.ebi.ac.uk/pdbsum/3zx6 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 22: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ecoli]] | [[Category: Ecoli]] | ||
[[Category: Ferris, H U | [[Category: Ferris, H U]] | ||
[[Category: Lupas, A L | [[Category: Lupas, A L]] | ||
[[Category: Zeth, K | [[Category: Zeth, K]] | ||
[[Category: Fusion]] | [[Category: Fusion]] | ||
[[Category: Hamp domain]] | [[Category: Hamp domain]] | ||
[[Category: Signaling]] | [[Category: Signaling]] | ||
[[Category: Tsr receptor]] | [[Category: Tsr receptor]] | ||
Revision as of 12:55, 4 January 2015
Structure of Hamp(AF1503)-Tsr fusion - Hamp (A291V) mutantStructure of Hamp(AF1503)-Tsr fusion - Hamp (A291V) mutant
Structural highlights
Publication Abstract from PubMedBacterial chemotaxis receptors are elongated homodimeric coiled-coil bundles, which transduce signals generated in an N-terminal sensor domain across 15-20nm to a conserved C-terminal signaling subdomain. This signal transduction regulates the activity of associated kinases, altering the behavior of the flagellar motor and hence cell motility. Signaling is in turn modulated by selective methylation and demethylation of specific glutamate and glutamine residues in an adaptation subdomain. We have determined the structure of a chimeric protein, consisting of the HAMP domain from Archaeoglobus fulgidus Af1503 and the methyl-accepting domain of Escherichia coli Tsr. It shows a 21nm coiled coil that alternates between two coiled-coil packing modes: canonical knobs-into-holes and complementary x-da, a variant form related to the canonical one by axial rotation of the helices. Comparison of the obtained structure to the Thermotoga maritima chemoreceptor TM1143 reveals that they adopt different axial rotation states in their adaptation subdomains. This conformational change is presumably induced by the upstream HAMP domain and may modulate the affinity of the chemoreceptor to the methylation-demethylation system. The presented findings extend the cogwheel model for signal transmission to chemoreceptors. Axial helix rotation as a mechanism for signal regulation inferred from the crystallographic analysis of the E. coli serine chemoreceptor.,Ferris HU, Zeth K, Hulko M, Dunin-Horkawicz S, Lupas AN J Struct Biol. 2014 Mar 27. pii: S1047-8477(14)00068-9. doi:, 10.1016/j.jsb.2014.03.015. PMID:24680785[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||