Structure of Rab GDP-Dissociation Inhibitor in Complex with Prenylated YPT1 GTPase

Science

Volumn 302, Issue 5645, 2003, Pages 646-650

  Rak, Alexey ^a   Pylypenko, Olena ^b   Durek, Thomas ^a   Watzke, Anja ^a   Kushnir, Susanna ^a   Brunsveld, Lucas ^a   Waldmann, Herbert ^a,c   Goody, Roger S ^a   Alexandrov, Kirill ^a  

^a MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

^b MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH   (Germany)

^c TU DORTMUND UNIVERSITY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; DISSOCIATION; HYDROPHOBICITY; PROTEINS; SYNTHESIS (CHEMICAL);

EUKARYOTIC CELLS;

ENZYME INHIBITION;

ISOPRENOID; NUCLEOTIDE; PROTEIN; RAB GUANOSINE DIPHOSPHATE DISSOCIATION INHIBITOR; RAB PROTEIN; UNCLASSIFIED DRUG; YPT GUANOSINE TRIPHOSPHATASE; YPT1 GUANOSINE TRIPHOSPHATASE;

BIOLOGY; MUTATION; PROTEIN;

ARTICLE; BINDING SITE; CHEMICAL ANALYSIS; CONFORMATIONAL TRANSITION; CRYSTALLIZATION; EUKARYOTIC CELL; HYDROGEN BOND; HYDROPHOBICITY; MENTAL DEFICIENCY; NUCLEOTIDE SEQUENCE; PRENYLATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN ENGINEERING; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; GUANINE NUCLEOTIDE DISSOCIATION INHIBITORS; GUANOSINE DIPHOSPHATE; HYDROGEN BONDING; HYDROPHOBICITY; LIPID METABOLISM; MAGNESIUM; MODELS, MOLECULAR; MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN ISOPRENYLATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RAB GTP-BINDING PROTEINS; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE PROTEINS;

EUKARYOTA;

EID: 0142178212     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1087761     Document Type: Article

References (27)

1. S. R. Pfeffer, Trends Cell Biol. 11, 487 (2001).
2. N. Segev, Curr. Opin. Cell Biol. 13, 500 (2001).
3. M. Zerial, H. McBride, Nature Rev. Mol. Cell Biol. 2, 107 (2001).
4. C. Alory, W. E. Balch, Traffic 2, 532 (2001).
5. 92 is replaced by Pro (I92P). Single-letter abbreviations for the amino acid residues are as follows: A, Ala; C, Cys; D, Asp; E, Glu; F, Phe; G, Gly; H, His; I, Ile; K, Lys; L, Leu; M, Met; N, Asn; P. Pro; Q, Gln; R, Arg; S, Ser; T. Thr; V, Val; W, Trp; and Y, Tyr.
6. M. D. Garrett, J. E. Zahner, C. M. Cheney, P. J. Novick, EMBO J. 13, 1718 (1994).
7. P. D'Adamo et al., Nature Genet. 19, 134 (1998).
8. I. Schalk et al., Nature 381, 42 (1996).
9. Y. An et al., Structure (Cambridge) 11, 347 (2003).
10. H. Horiuchi, O. Ullrich, C. Bucci, M. Zerial, Methods Enzymol. 257, 9 (1995).
11. A. Kalinin et al., Protein Expr. Purif. 22, 84 (2001).
12. K. Alexandrov et al., J. Am. Chem. Soc. 124, S648 (2002).
13. B. Ludolph, F. Eisele, M. Waldeman, J. Am. Chem. Soc. 124, S954 (2002).
14. T. W. Muir, Annu. Rev. Biochem. 72, 249 (2003).
15. A. T. Constantinescu et al., Structure (Cambridge) 10, S69 (2002).
16. P. Chavrier et al., Nature 353, 769 (1991).
17. A. Rak, K. Alexandrov, unpublished observations.
18. P. A. Borlack-Sjodin. S. M. Margarit, D. Bar-Sagi, J. Kuriyan. Nature 394, 337 (1998).
19. G. R. Hoffman, N. Nassar, R. A. Cerione, Cell 100, 345 (2000).
20. O. Pylypenko et al., Mol. Cell 11, 483 (2003).
21. C. S. Ricard et al., Genesis 31, 17 (2001).
22. P. M. Gilbert, C. G. Burd, J. Biol. Chem. 276, 8014 (2001).
23. F. Shen, M. C. Seabra. J. Biol. Chem. 271, 3692 (1996).
24. T. Sakisaka, T. Meerlo, J. Matteson, H. Plutner, W. E. Balch, EMBO J. 21. 6125 (2002).
25. P. Luan et al., Traffic 1, 270 (2000).
26. A. T. Brunger et al., Acta Crystallogr. D Biol. Clystallogr. 54 (Pt. 5), 905 (1998).
27. G. Holtermann is acknowledged for invaluable technical assistance. We thank the staff of SLS beamline at Paul Scherrer Institute, Villingen. for help during data collection. We thank I. Schlichting and W. Blankenfeldt for help with data collection and A.-C. Ceacareanu for help with construction of expression vectors. D. Gallwitz is acknowledged for a generous gift of anti-Ypt1 antibody. W. Blankenfeldt is gratefully acknowledged for critically reading the manuscript and stimulating discussions. A.R. was supported by an Engelhorn foundation long-term postdoctoral fellowship. L.B. was supported by postdoctoral fellowship of the Alexander von Humboldt Foundation. This work was supported in part by grant DFG AL 484/S-2 to K.A. and grant 1/77 977 of the Volkswagen foundation to K.A., R.S.G., and H.W. Coordinates have been deposited in the Protein Data Bank (Brookhaven National Laboratory) with accession number 1URV.