Malarial EBA-175 Region VI Crystallographic Structure Reveals a KIX-Like Binding Interface

Journal of Molecular Biology

Volumn 375, Issue 3, 2008, Pages 773-781

  Withers Martinez, Chrislaine ^a   Haire, Lesley F ^a   Hackett, Fiona ^a   Walker, Philip A ^a   Howell, Steven A ^a   Smerdon, Stephen J ^a   Dodson, Guy G ^a   Blackman, Michael J ^a  

^a NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

Author keywords

CBP KIX; crystal structure; EBA 175; Plasmodium falciparum; region VI

Indexed keywords

BINDING PROTEIN; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; CYSTEINE; DISULFIDE; DUFFY BINDING PROTEIN; HOMODIMER; PROTEIN EBA 175; PROTEIN SUBUNIT; PROTOZOAL PROTEIN; SELENOMETHIONINE; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DIMERIZATION; ERYTHROCYTE; MALARIA; NONHUMAN; PLASMODIUM FALCIPARUM; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; TIGHT JUNCTION;

PLASMODIUM FALCIPARUM; VERTEBRATA;

EID: 37349056078     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.10.071     Document Type: Article

References (44)

1. Adams J.H., Hudson D.E., Torii M., Ward G.E., Wellems T.E., Aikawa M., and Miller L.H. The Duffy receptor family of Plasmodium knowlesi is located within the micronemes of invasive malaria merozoites. Cell 63 (1990) 141-153
2. Adams J.H., Blair P.L., Kaneko O., and Peterson D.S. An expanding ebl family of Plasmodium falciparum. Trends Parasitol. 17 (2001) 297-299
3. Michon P., Stevens J.R., Kaneko O., and Adams J.H. Evolutionary relationships of conserved cysteine-rich motifs in adhesive molecules of malaria parasites. Mol. Biol. Evol. 19 (2002) 1128-1142
4. Chitnis C.E. Molecular insights into receptors used by malaria parasites for erythrocyte invasion. Curr. Opin. Hematol. 8 (2001) 85-91
5. Singh A.P., Ozwara H., Kocken C.H., Puri S.K., Thomas A.W., and Chitnis C.E. Targeted deletion of Plasmodium knowlesi Duffy binding protein confirms its role in junction formation during invasion. Mol. Microbiol. 55 (2005) 1925-1934
6. Chitnis C.E., and Miller L.H. Identification of the erythrocyte binding domains of Plasmodium vivax and Plasmodium knowlesi proteins involved in erythrocyte invasion. J. Exp. Med. 180 (1994) 497-506
7. Sim B.K., Chitnis C.E., Wasniowska K., Hadley T.J., and Miller L.H. Receptor and ligand domains for invasion of erythrocytes by Plasmodium falciparum. Science 264 (1994) 941-944
8. VanBuskirk K.M., Sevova E., and Adams J.H. Conserved residues in the Plasmodium vivax Duffy-binding protein ligand domain are critical for erythrocyte receptor recognition. Proc. Natl Acad. Sci. USA 101 (2004) 15754-15759
9. Singh S.K., Singh A.P., Pandey S., Yazdani S.S., Chitnis C.E., and Sharma A. Definition of structural elements in Plasmodium vivax and P. knowlesi Duffy-binding domains necessary for erythrocyte invasion. Biochem. J. 374 (2003) 193-198
10. Hans D., Pattnaik P., Bhattacharyya A., Shakri A.R., Yazdani S.S., Sharma M., et al. Mapping binding residues in the Plasmodium vivax domain that binds Duffy antigen during red cell invasion. Mol. Microbiol. 55 (2005) 1423-1434
11. Singh S.K., Hora R., Belrhali H., Chitnis C.E., and Sharma A. Structural basis for Duffy recognition by the malaria parasite Duffy-binding-like domain. Nature 439 (2006) 741-744
12. Tolia N.H., Enemark E.J., Sim B.K., and Joshua-Tor L. Structural basis for the EBA-175 erythrocyte invasion pathway of the malaria parasite Plasmodium falciparum. Cell 122 (2005) 183-193
13. O'Donnell R A., Hackett F., Howell S.A., Treeck M., Struck N., Krnajski Z., et al. Intramembrane proteolysis mediates shedding of a key adhesin during erythrocyte invasion by the malaria parasite. J. Cell Biol. 174 (2006) 1023-1033
14. Gilberger T.W., Thompson J.K., Reed M.B., Good R.T., and Cowman A.F. The cytoplasmic domain of the Plasmodium falciparum ligand EBA-175 is essential for invasion but not protein trafficking. J. Cell Biol. 162 (2003) 317-327
15. Treeck M., Struck N.S., Haase S., Langer C., Herrmann S., Healer J., et al. A conserved region in the EBL proteins is implicated in microneme targeting of the malaria parasite Plasmodium falciparum. J. Biol. Chem. 281 (2006) 31995-32003
16. Radhakrishnan I., Perez-Alvarado G.C., Parker D., Dyson H.J., Montminy M.R., and Wright P.E. Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions. Cell 91 (1997) 741-752
17. Parker D., Ferreri K., Nakajima T., LaMorte V.J., Evans R., Koerber S.C., et al. Phosphorylation of CREB at Ser-133 induces complex formation with CREB-binding protein via a direct mechanism. Mol. Cell. Biol. 16 (1996) 694-703
18. Larsson A.M., Stahlberg J., and Jones T.A. Preparation and crystallization of selenomethionyl dextranase from Penicillium minioluteum expressed in Pichia pastoris. Acta Crystallogr. Sect. D 58 (2002) 346-348
19. Wang J., Dauter M., and Dauter Z. What can be done with a good crystal and an accurate beamline?. Acta Crystallogr. Sect. D 62 (2006) 1475-1483
20. Young L., Jernigan R.L., and Covell D.G. A role for surface hydrophobicity in protein-protein recognition. Protein Sci. 3 (1994) 717-729
21. Koide A., Gilbreth R.N., Esaki K., Tereshko V., and Koide S. High-affinity single-domain binding proteins with a binary-code interface. Proc. Natl Acad. Sci. USA 104 (2007) 6632-6637
22. Copley R.R., and Barton G.J. A structural analysis of phosphate and sulphate binding sites in proteins. Estimation of propensities for binding and conservation of phosphate binding sites. J. Mol. Biol. 242 (1994) 321-329
23. Holm L., and Sander C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233 (1993) 123-138
24. Yang F., Vought B.W., Satterlee J.S., Walker A.K., Jim Sun Z.Y., Watts J.L., et al. An ARC/mediator subunit required for SREBP control of cholesterol and lipid homeostasis. Nature 442 (2006) 700-704
25. Kaneko O., Fidock D.A., Schwartz O.M., and Miller L.H. Disruption of the C-terminal region of EBA-175 in the Dd2/Nm clone of Plasmodium falciparum does not affect erythrocyte invasion. Mol. Biochem. Parasitol. 110 (2000) 135-146
26. Reed M.B., Caruana S.R., Batchelor A.H., Thompson J.K., Crabb B.S., and Cowman A.F. Targeted disruption of an erythrocyte binding antigen in Plasmodium falciparum is associated with a switch toward a sialic acid-independent pathway of invasion. Proc. Natl Acad. Sci. USA 97 (2000) 7509-7514
27. Zor T., De Guzman R.N., Dyson H.J., and Wright P.E. Solution structure of the KIX domain of CBP bound to the transactivation domain of c-Myb. J. Mol. Biol. 337 (2004) 521-534
28. De Guzman R.N., Goto N.K., Dyson H.J., and Wright P.E. Structural basis for cooperative transcription factor binding to the CBP coactivator. J. Mol. Biol. 355 (2006) 1005-1013
29. Keller P., and Simons K. Post-Golgi biosynthetic trafficking. J. Cell Sci. 110 (1997) 3001-3009
30. Pizarro J.C., Normand B.V., Chesne-Seck M.L., Collins C.R., Withers-Martinez C., Hackett F., et al. Crystal structure of the malaria vaccine candidate apical membrane antigen 1. Science 308 (2005) 408-411
31. Howell S.A., Well I., Fleck S.L., Kettleborough C., Collins C.R., and Blackman M.J. A single malaria merozoite serine protease mediates shedding of multiple surface proteins by juxtamembrane cleavage. J. Biol. Chem. 278 (2003) 23890-23898
32. Lilius G., Persson M., Bulow L., and Mosbach K. Metal affinity precipitation of proteins carrying genetically attached polyhistidine affinity tails. Eur. J. Biochem. 198 (1991) 499-504
33. Otwinowski Z., and Minor W. Processing of X-ray diffraction data collected in oscillation mode. In: Carter C.W.J., and Sweet R.M. (Eds). Methods in Enzymology: Macromolecular Crystallography vol. 276 (1997), Academic Press, New York 307-326
34. Uson I., and Sheldrick G.M. Advances in direct methods for protein crystallography. Curr. Opin. Struct. Biol. 9 (1999) 643-648
35. Otwinowski Z. In: Wolf W., Evans P.R., and Leslie A.G.W. (Eds). Isomorphous replacement and anomalous scattering (1991), Daresbury Laboratory, Warrington 80
36. Wang J.W., Chen J.R., Gu Y.X., Zheng C.D., and Fan H.F. Direct-method SAD phasing with partial-structure iteration: towards automation. Acta Crystallogr. Sect. D 60 (2004) 1991-1996
37. Cowtan K. Joint CCP4 and ESF-EACBM newsletter on protein. Crystallography 31 (1994) 34-38
38. Terwilliger T.C. Automated main-chain model building by template matching and iterative fragment extension. Acta Crystallogr. Sect. D 59 (2003) 38-44
39. Lamzin V.S., Perrakis A., and Wilson K.S. The ARP/WARP suite for automated construction and refinement of protein models. In: Rossmann M.G., and Arnold E. (Eds). International Tables for Crystallography vol. F (2001), Kluwer Academic Publishers, Dordrecht, The Netherlands 720-722
40. Emsley P., and Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr. Sect. D 60 (2004) 2126-2132
41. Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. Sect. D 53 (1997) 240-255
42. Laskowski R.A., Rullmannn J.A., MacArthur M.W., Kaptein R., and Thornton J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8 (1996) 477-486
43. Lovell S.C., Davis I.W., Arendall III W.B., de Bakker P.I., Word J.M., Prisant M.G., et al. Structure validation by Calpha geometry: phi, psi and Cbeta deviation. Proteins: Struct. Funct. Genet. 50 (2003) 437-450
44. DeLano W.L. The PyMOL Molecular Graphics System (2002), DeLano Scientific, Palo Alto, CA, USA. http://www.pymol.org http://www.pymol.org