Crystal structure of the GAP domain of Gyp1p: first insights into interaction with Ypt/Rab proteins
Copyright policy )Crystal structure of the GAP domain of Gyp1p: first insights into interaction with Ypt/Rab proteins
We present the 1.9 A resolution crystal structure of the catalytic domain of Gyp1p, a specific GTPase activating protein (GAP) for Ypt proteins, the yeast homologues of Rab proteins, which are involved in vesicular transport. Gyp1p is a member of a large family of eukaryotic proteins with shared sequence motifs. Previously, no structural information was available for any member of this class of proteins. The GAP domain of Gyp1p was found to be fully alpha-helical. However, the observed fold does not superimpose with other alpha-helical GAPs (e.g. Ras- and Cdc42/Rho-GAP). The conserved and catalytically crucial arginine residue, identified by mutational analysis, is in a comparable position to the arginine finger in the Ras- and Cdc42-GAPs, suggesting that Gyp1p utilizes an arginine finger in the GAP reaction, in analogy to Ras- and Cdc42-GAPs. A model for the interaction between Gyp1p and the Ypt protein satisfying biochemical data is given.
- Max Planck Society Germany
- University of Queensland Australia
- University of Queensland Australia
- University of Göttingen Germany
- Queensland University of Technology Australia
Gtpase-Activating Protein, Models, Molecular, Identification, Protein Folding, Saccharomyces cerevisiae Proteins, GTPase activating protein, Amino Acid Motifs, Molecular Sequence Data, Transport, Arginine, Crystallography, X-Ray, Rab protein, Complex, Catalytic Domain, vesicular transport, Family, Amino Acid Sequence, cdc42 GTP-Binding Protein, Saccharomyces cerevisiae, Guanylyl Imidodiphosphate, GTPase-Activating Proteins, Diffraction Data, Ypt-GAP domain, Yeast, rab GTP-Binding Proteins, ras GTPase-Activating Proteins, Prediction, Member, Sequence Alignment, Ras
Gtpase-Activating Protein, Models, Molecular, Identification, Protein Folding, Saccharomyces cerevisiae Proteins, GTPase activating protein, Amino Acid Motifs, Molecular Sequence Data, Transport, Arginine, Crystallography, X-Ray, Rab protein, Complex, Catalytic Domain, vesicular transport, Family, Amino Acid Sequence, cdc42 GTP-Binding Protein, Saccharomyces cerevisiae, Guanylyl Imidodiphosphate, GTPase-Activating Proteins, Diffraction Data, Ypt-GAP domain, Yeast, rab GTP-Binding Proteins, ras GTPase-Activating Proteins, Prediction, Member, Sequence Alignment, Ras
citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).86 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Top 10% influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Top 10% impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Top 10%
Citations provided by BIP!Popularity provided by BIP!