3ZX6: Structure Of Hamp(af1503)-tsr Fusion - Hamp (a291v) Mutant

Bacterial 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.
PDB ID: 3ZX6Download
MMDB ID: 97674
PDB Deposition Date: 2011/8/8
Updated in MMDB: 2014/06
Experimental Method:
x-ray diffraction
Resolution: 2.65  Å
Similar Structures:
Biological Unit for 3ZX6: dimeric; determined by software (PISA)
Molecular Components in 3ZX6
Label Count Molecule
Proteins (2 molecules)
Hamp, Methyl-accepting Chemotaxis Protein I(Gene symbol: tsr)
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB