3kxi

crystal structure of SsGBP and GDP complex

spinqualitylabelsall models 3kxi, resolution 2.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3kxi is a 1 chain structure with sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GDP, MG, SCN Related: 2qth, 3kxk, 3kxl Gene: hflX, SSO0269 (Sulfolobus solfataricus) Resources: FirstGlance, OCA, RCSB, PDBsum Function [Q980M3_SULSO] GTPase that associates with the 50S ribosomal subunit and may have a role during protein synthesis or ribosome biogenesis. Specific for GTP. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed GTPase domains from members of the HflX protein family have their catalytic glutamine residue of the DxxGQ motif substituted by phenylalanine, while they are still able to hydrolyse GTP. This appears to challenge the traditional view of GTP hydrolysis mechanism of Ras-like GTPases. SsGBP from the hyperthermophilic archaeon Sulfolobus solfataricus provided the first crystal structure of the HflX family. Here, we report structure-based mutagenesis analyses on SsGBP. Six-point mutations were individually introduced in the Ras-like GTPase domain including regions of P-loop, switches I and II. Intrinsic GTPase activities and thermal stabilities of these variants together with the wild-type full-length SsGBP and its isolated GTPase domain were analysed. Both functional and structural analyses of G235P and G235S mutants, which showed total and partial loss of the GTP hydrolyzing activity, respectively, support our hypothesis that the role of aligning a nucleophilic water molecule by the Ras Gln60 residue is replaced by the backbone amide group of Gly235 in SsGBP. Together with functional studies of other mutants, we conclude that the classical view of GTP hydrolysis mechanism likely remains the same in the HflX family with a twist in the entity of the nucleophilic alignment. Functional study on GTP hydrolysis by the GTP-binding protein from Sulfolobus solfataricus, a member of the HflX family.,Huang B, Wu H, Hao N, Blombach F, van der Oost J, Li X, Zhang XC, Rao Z J Biochem. 2010 Jul;148(1):103-13. Epub 2010 Apr 16. PMID:20400571 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also GTP-binding protein

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