Crystal structure of the phosphatidylethanolamine-binding protein from bovine brain: A novel structural class of phospholipid-binding proteins

Structure

Volumn 6, Issue 10, 1998, Pages 1255-1265

  Serre, Laurence ^a,b   Vallée, Béatrice ^a,b   Bureaud, Nicole ^a,b   Schoentgen, Françoise ^a,b   Zelwer, Charles ^a,b  

^a CNRS   (France)

^b UNIVERSITÉ D'ORLÉANS   (France)

Author keywords

Cis peptide; Crystal; Greek key; Phospholipid; Protein

Indexed keywords

ANIMALIA; BOS TAURUS; BOVINAE; EUKARYOTA;

EID: 0032532743     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(98)00126-9     Document Type: Article

References (53)

1. Bernier, I. & Jollès, P. (1984). Purification and characterization of a basic 23 kDa cytosolic protein from bovine brain. Biochem. Biophys. Acta 790, 174-181.
2. Bernier, I., Fresca, J.P. & Jollès, P. (1986). Ligand-binding studies with a 23 kDa protein purified from bovine brain cytosol. Biochem. Biophys. Acta 871, 19-23.
3. Bucquoy, S., Jollès, P. & Schoentgen, F. (1994). Relationships between molecular interactions (nucleotides, lipids and proteins) and structural features of the bovine brain 21-23 kDa protein. Eur. J. Biochem. 225, 1203-1210.
4. Bollengier, F. & Mahler, A. (1988). Location of the novel neuropeptide h3 in subsets of tissues from different species. J. Neurochem. 50, 1210-1214.
5. Hori, N., et al., & Matsubara, K. (1994). A human cDNA sequence homologue of bovine phosphatidylethanolamine-binding protein. Gene 140, 293-294.
6. Seddiqi, N., et al., & Schoentgen, F. (1994). Amino sequence of the homo sapiens brain 21-23 kDa protein (neuropolypeptide h3) comparison with its counterparts from Rattus norvegicus and Bos taurus species, and expression of its mRNA in different tissues. J. Mol. Evol. 39, 655-660.
7. Moore, C., Perry, A.C.F., Love, S. & Hall, L. (1996). Sequence analysis and immunolocalisation of phosphatidylethanolamine binding protein (PBP) in human brain tissue. Mol. Brain Res. 37, 74-78.
8. Perry, A.C.F., Hall, L., Bell, A.E. & Jones, R. (1994). Sequence analysis of a mammalian phospholipid-binding protein from testis and epididymis and its distribution between spermatozoa and extracellular secretions. Biochem. J. 301, 235-242.
9. Grandy, D.K., Hanneman, E., Bunzow, J., Shih, M., Machida, C.A., Bidlack, J.M. & Civelli, O. (1990). Purification, cloning and tissue distribution of a 23 kDa rat protein isolated by morphine affinity chromatography. Mol. Endocrinol. 4, 1370-1376.
10. Schoentgen, F., Saccoccio, F., Jollès, J., Bernier, I. & Jollès, P. (1987). Complete amino acid sequence of a basic 21-kDa protein from bovine brain cytosol. Eur. J. Biochem. 166, 333-338.
11. Pikielny, C.W., Hasan, G., Rouyer, F. & Rosbash, M. (1994). Members of a family of Drosophila putative odorant-binding proteins are expressed in different subsets of olfactory hairs. Neuron 12, 35-49.
12. Lobos, E., Altmann, M., Mengod, G., Weiss, N., Rudin, W. & Karam, M. (1990). Identification of an Onchocerca volvulus cDNA encoding a low molecular weight antigen recognized by onchocerciasis patient sera. Mol. Biochem. Parasitol. 39, 135-146.
13. Gems, D., et al., & Maizels, R.M. (1995). An abundant trans-spliced mRNA from Toxocara canis infective larvae encodes a 26-kDa protein with homology to phosphatidylethanolamine-binding proteins. J. Biol. Chem. 270, 18517-18522.
14. Robinson, L.C. & Tatchell, K. (1991). TFS1: a suppressor of CDC25 mutation in Saccharomyces cerevisiae. Mol. Gen. Genet 230, 241-250.
15. Bradley, D., Carpenter, R., Copsey, L., Vincent, C., Rothstein, S. & Coen, E. (1996). Control of inflorescence architecture in Antirrhinum. Nature 379, 791-797.
16. Trottein, F. & Cowman, A.F. (1995). The primary structure of a putative phosphatidylethanolamine binding protein from Plasmodium falciparum. Mol. Biochem. Parasitol. 70, 235-239.
17. Schoentgen, F., et al., & Mornon, J.P. (1992). Main structural and functional features of the basic cytosolic bovine 21 kDa protein delineated from hydrophobic cluster analysis and molecular modeling. Protein Eng. 5, 295-303.
18. Rossmann, M.G., Moras, D. & Olsen, K.W. (1974). Chemical and biological evolution of a nucleotide-binding protein. Nature 250, 194-199.
19. Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 97, 110-119.
20. Laskowski, R.A., MacArthur, M.W., Moss, D.S. & Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
21. Kabsch, W. & Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637.
22. Holm, L. & Sander, C. (1993). Protein structure comparison by alignment of distance matrix. J. Mol. Biol. 233, 123-138.
23. Gosser, Y.Q., et al., & Rosen, M.K. (1997). C-terminal binding domain of the Rho GDP-dissociation inhibitor directs N-terminal inhibitory peptide to GTPases. Nature. 387, 814-819.
24. Kleywegt, G.J. & Jones, T.A. (1994). Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Cryst. D 50, 178-185.
25. Nicholls, A., Sharp, K. & Honig, B. (1992). Manual for version 1.04. GRASP: graphical representation and analysis of surface properties.
26. Pai, E.F., Krengel, U., Holmes, K.C., John, J. & Wittinghofer, A. (1989). Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation. Nature 341, 209-214.
27. Sha, B., Phillips, S.E, Bankaitis, V.A. & Luo, M. (1998). Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein. Nature 391, 506-510.
28. Flower, J. (1996). The lipocalin family: structure and function. Biochem. J. 318, 1-14.
29. Shin, D.H., Lee, J.Y., Hwang, K.Y., Kim, K.K. & Suh, S.W. (1995). High-resolution structure of a non-specific lipid-transfer protein from maize seedlings. Structure 3, 189-199.
30. Stewart, D.E., Sarkar, A. & Wampler, J.E. (1990). Occurrence and role of cis peptide bonds in protein structures. J. Mol. Biol. 214, 253-260.
31. Herzberg, O. & Moult, J. (1991). Analysis of the steric strain in the polypeptide backbone of protein molecules. Proteins 11, 223-229.
32. Fisher, A.J., Thompson, T.B., Thoden, J.B., Baldwin, T.O. & Rayment, I. (1996). The 1.5 Å resolution crystal structure of bacterial luciferase in low salt conditions. J. Biol. Chem. 271, 21956-21968.
33. Perisic, O., Fong, S., Lynch, D.E., Bycroft, M. & Williams, R.L. (1998). Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2. J. Biol. Chem. 273, 1596-1604.
34. Bradley, D., Ratcliffe, O., Vincent, C., Carpenter, R. & Coen, E. (1997). Inflorescence commitment and architecture in Arabidopsis. Science 275, 80-83.
35. Wlodawer, A., Bott, R. & Sjolin, L. (1982). The refined crystal structure of ribonuclease A at 2.0 Å resolution. J. Biol. Chem. 257, 1352-1332.
36. + reductase: prototype for a structurally novel flavoenzyme. Science 251, 60-66.
37. 2+/phospholipid fold. Cell 80, 929-938.
38. Essen, L.O., Perisic, O., Cheung, R., Katan, M. & Williams, R.L. (1996). Crystal structure of a mammalian phosphoinoside-specific phospholipase C delta. Nature 380, 595-602.
39. Bruun, A.W., Svendsen, I., Sorensen, S.O., Kielland-Brandt, M.C. & Winther, J.C. (1998). A high affinity-inhibitor of yeast carboxypeptidase Y is encoded by TFS1 and shows homology to a family of lipid binding proteins. Biochemistry 37, 3351-3357.
40. Leslie, A.G.W. (1990). Crystallography Computing. Oxford University Press, UK.
41. Evans P.R. (1993). Data reduction. In Proceedings of the CCP4 Study Weekend on Data Collection and Processing, pp. 114-122, SERC Laboratory, Daresbury, Warrington, UK.
42. Collaborative Computational Project No. 4. (1994). The CCP4 suite; programs for protein crystallography. Acta Cryst. D 50, 760-763.
43. La Fortelle, E. & Bricogne, G. (1997). Maximum-likelihood parameter refinement program for MIR and MAD phasing. Methods Enzymol. 276, 472-494.
44. 1 ATPase. Acta Cryst. D 52, 30-42.
45. Brünger, A.T. (1992). The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-474.
46. Brünger, A.T. (1992). X-PLOR Version 3.1: a System for X-ray Crystallography and NMR. Yale University Press, New Haven, USA.
47. Murshudov, G., Vagin, A.A. & Dodson, E.J. (1997). Refinement of molecular structures by the maximum-likelihood method. Acta Cryst. D 53, 240-255.
48. Lamzin, V.S. & Wilson, K.S. (1993). Automated refinement of protein models. Acta Cryst. D 49, 129-147.
49. Navaza, J. (1993). On the computation of the fast rotation function. Acta Cryst. D 49, 588-591.
50. Carson, M. (1997). Ribbons. Methods Enzymol. 277, 493-505.
51. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst. 24, 946-950.
52. Read, J.R. (1986). Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Cryst. A 42, 140-149.
53. Johnston, M., et al., & Hoheisel, J.D. (1997). The nucleotide sequence of Saccharomyces cerevisiae chromosome XII. Nature 387, 87-90.