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Publication Abstract from PubMed

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.

An atypical receiver domain controls the dynamic polar localization of the Myxococcus xanthus social motility protein FrzS.,Fraser JS, Merlie JP Jr, Echols N, Weisfield SR, Mignot T, Wemmer DE, Zusman DR, Alber T Mol Microbiol. 2007 Jul;65(2):319-32. Epub 2007 Jun 15. PMID:17573816^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.