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- W2023551322 abstract "Two new structures of the SRP GTPase Ffh have been determined at 1.1 A resolution and provide the basis for comparative examination of the extensive water structure of the apo conformation of these GTPases. A set of well defined water-binding positions have been identified in the active site of the two-domain ;NG' GTPase, as well as at two functionally important interfaces. The water hydrogen-bonding network accommodates alternate conformations of the protein side chains by undergoing local rearrangements and, in one case, illustrates binding of a solute molecule within the active site by displacement of water molecules without further disruption of the water-interaction network. A subset of the water positions are well defined in several lower resolution structures, including those of different nucleotide-binding states; these appear to function in maintaining the protein structure. Consistent arrangements of surface water between three different ultrahigh-resolution structures provide a framework for beginning to understand how local water structure contributes to protein-ligand and protein-protein binding in the SRP GTPases." @default.
- W2023551322 created "2016-06-24" @default.
- W2023551322 creator A5082877660 @default.
- W2023551322 creator A5091701765 @default.
- W2023551322 date "2006-11-23" @default.
- W2023551322 modified "2023-09-23" @default.
- W2023551322 title "Analysis of protein hydration in ultrahigh-resolution structures of the SRP GTPase Ffh" @default.
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- W2023551322 doi "https://doi.org/10.1107/s0907444906040807" @default.
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