The dynamic behavior of CheW from Thermotoga maritima in solution, as determined by nuclear magnetic resonance: implications for potential protein-protein interaction sites.

Measurements of the 15N relaxation parameters have been used to characterize the backbone dynamics of CheW from Thermotoga maritima. The dynamic nature of residues that appeared disordered in our recent solution structure of CheW is confirmed by these dynamics measurements. We have interpreted the data in terms of the Lipari and Szabo 'model-free' approach. The derived order parameter, S(2), the [1H]-(15)N heteronuclear nuclear Overhauser effect (NOE) values, the chemical exchange rate, R(ex), and the internal correlation time, tau(e), show that CheW exhibits considerable motional freedom from the picosecond to millisecond time scales. These regions of the protein cluster within the framework of the three-dimensional structure and may indicate possible binding sites for other protein components of the bacterial chemotaxis receptor-signaling complex. The structure of CheW consists of two five-stranded beta-barrel domains that pack together with an extensive hydrophobic core between the domains. Regions highlighted by dynamics measurements co-localize to specific regions of the three-dimensional structure of CheW previously implicated in the formation of bacterial chemotaxis receptor signaling complex. The motional properties of domain 2 of CheW suggest that this domain may be able to experience structural rearrangements that allow the exposure of a hydrophobic surface area that could be used as a binding surface for the other members of the receptor complex. Residues within domain 2 have been implicated in binding interactions for two chemotaxis proteins, CheA and the receptor. We further propose that domain 1 interacts with other components of the chemotaxis machinery, such as CheZ, or in the formation of clusters of signaling components. Copyright 2002 Elsevier Science B.V.