Abstract
Tailspike proteins play an important role in the bacteriophage's infection process and have become classic models for the study of folding of large proteins. The phage P22 tailspike protein recognizes and cleaves O-antigen polysaccharides on the membrane of bacteria in an extended binding cleft, thus allowing for the injection of phage DNA into the cell. In general, very little is known of the interaction processes of these larger proteins because of a lack of both structural and thermodynamic data. Here, we apply multiple solvent crystal structures (MSCS), a crystallographic method that utilizes organic solvents as functional group probes to protein binding surfaces. Protein crystals are soaked in a number of organic solvents then solved and superimposed in order to identify clusters of organic solvent binding as well as providing a more detailed picture of protein plasticity and hydration than is possible in a single structure. Twelve binding sites are described, with locations ranging from known carbohydrate binding pockets to hot-spots on the protein surface that have not been previously characterized. MSCS also allows us to qualitatively assess the nature of structural water molecules that reside in the active site cleft and have been shown to play an integral role in substrate binding. This research was supported by the NSF (MCB - 1237512) grant.
Published Version
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