| Autor: |
Ramirez UD; Department of Molecular Pharmacology and Biological Chemistry, Northwestern University, Chicago, IL 60611, USA., Freymann DM |
| Jazyk: |
angličtina |
| Zdroj: |
Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 2006 Dec; Vol. 62 (Pt 12), pp. 1520-34. Date of Electronic Publication: 2006 Nov 23. |
| DOI: |
10.1107/S0907444906040807 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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