2NT4

Receiver domain from Myxococcus xanthus social motility protein FrzS (H92F mutant)

Summary for 2NT4

• Entry DOI: 10.2210/pdb2nt4/pdb
• Related: 2gkg 2i6f 2nt3
• Descriptor: Response regulator homolog, CHLORIDE ION (3 entities in total)
• Functional Keywords: social motility, signaling, receiver domain, two-component, signaling protein
• Biological source: Myxococcus xanthus
• Total number of polymer chains: 1
• Total formula weight: 13731.00

Authors

Echols, N.,Fraser, J.,Weisfield, S.,Merlie, J.,Zusman, D.,Alber, T. (deposition date: 2006-11-06, release date: 2007-03-13, Last modification date: 2023-08-30)

Primary citation

Fraser, J.S.,Merlie, J.P.,Echols, N.,Weisfield, S.R.,Mignot, T.,Wemmer, D.E.,Zusman, D.R.,Alber, T.
An atypical receiver domain controls the dynamic polar localization of the Myxococcus xanthus social motility protein FrzS.
Mol.Microbiol., 65:319-332, 2007

PubMed Abstract: The Myxococcus xanthus FrzS protein transits from pole-to-pole within the cell, accumulating at the pole that defines the direction of movement in social (S) motility. Here we show using atomic-resolution crystallography and NMR that the FrzS receiver domain (RD) displays the conserved switch Tyr102 in an unusual conformation, lacks the conserved Asp phosphorylation site, and fails to bind Mg(2+) or the phosphoryl analogue, Mg(2+) x BeF(3). Mutation of Asp55, closest to the canonical site of RD phosphorylation, showed no motility phenotype in vivo, demonstrating that phosphorylation at this site is not necessary for domain function. In contrast, the Tyr102Ala and His92Phe substitutions on the canonical output face of the FrzS RD abolished S-motility in vivo. Single-cell fluorescence microscopy measurements revealed a striking mislocalization of these mutant FrzS proteins to the trailing cell pole in vivo. The crystal structures of the mutants suggested that the observed conformation of Tyr102 in the wild-type FrzS RD is not sufficient for function. These results support the model that FrzS contains a novel 'pseudo-receiver domain' whose function requires recognition of the RD output face but not Asp phosphorylation.

PubMed: 17573816
DOI: 10.1111/j.1365-2958.2007.05785.x

Experimental method

X-RAY DIFFRACTION (1.02 Å)