Structural Basis of Oligomannose Recognition by the Pterocarpus angolensis Seed Lectin

Journal of Molecular Biology

Volumn 335, Issue 5, 2004, Pages 1227-1240

  Loris, Remy ^a   Van Walle, Ivo ^a   De Greve, Henri ^a   Beeckmans, Sonia ^b   Deboeck, Francine ^b   Wyns, Lode ^a   Bouckaert, Julie ^a  

^a DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^b VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

Author keywords

Carbohydrate recognition; Lectin; Legume lectin; Mannose

Indexed keywords

CONCANAVALIN A; OLIGOMANNOSE; OLIGOSACCHARIDE; PLANT LECTIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBOHYDRATE ANALYSIS; COMPLEX FORMATION; CRYSTAL STRUCTURE; CRYSTALLIZATION; MOLECULAR RECOGNITION; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; PTEROCARPUS; STRUCTURE ANALYSIS; TREE;

BROSIMUM RUBESCENS; FABACEAE; MAACKIA AMURENSIS; PTEROCARPUS ANGOLENSIS; ULEX; ULEX EUROPAEUS;

EID: 0347284266     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.11.043     Document Type: Article

References (45)

1. Taylor M.E., Drickamer K. Introduction to Glycobiology. 2003;Oxford University Press, Oxford, UK.
2. Sharma V., Surolia A. Analyses of carbohydrate recognition by legume lectins: size of the combining site loops and their primary specificity. J. Mol. Biol. 267:1997;433-445.
3. Loris R., Hamelryck T., Bouckaert J., Wyns L. Legume lectin structure. Biochim. Biophys. Acta. 1383:1998;9-36.
4. Bouckaert J., Loris R., Poortmans F., Wyns L. The crystallographic structure of metal-free concanavalin A at 2.5 Å resolution. Proteins: Struct. Funct. Genet. 23:1995;510-540.
5. Bouckaert J., Dewallef Y., Poortmans F., Wyns L., Loris R. Structural dissection of the conformational pathways of de- and re-metallization of concanavalin A. J. Biol. Chem. 275:2000;19778-19787.
6. Lescar J., Loris R., Mitchell E., Gautier C., Chazalet V., Cox V., et al. Isolectins I-A and I-B of Griffonia (Bandeiria) simplicifolia: crystal structure of metal-free GSI-B4 and molecular bases for metal binding and monosaccharide specificity. J. Biol. Chem. 277:2002;6608-6614.
7. Manoj N., Srinivas V.R., Surolia A., Vijayan M., Suguna K. Carbohydrate specificity and salt-bridge mediated conformational change in acidic winged bean agglutinin. J. Mol. Biol. 302:2000;1129-1137.
8. Prabu M.M., Sankaranarayanan R., Puri K.D., Sharma V., Surolia A., Vijayan M., Suguna K. Carbohydrate specificity and quaternary association in basic winged bean lectin: X-ray analysis of the lectin at 2.5 Å resolution. J. Mol. Biol. 276:1998;787-796.
9. Audette G.F., Vandonselaar M., Delbaere L.T. The 2.2 Å resolution structure of the O(H) blood-group-specific lectin I from Ulex europaeus. J. Mol. Biol. 304:2000;423-433.
10. Rabijns A., Verboven C., Rouge P., Barre A., Van Damme E.J., Peumans W.J., De Ranter C.J. Structure of a legume lectin from the bark of Robinia pseudoacacia and its complex with N-acetylgalactosamine. Proteins: Struct. Funct. Genet. 44:2001;470-478.
11. Tempel W., Tschampel S., Woods R.J. The xenograft antigen bound to Griffonia simplicifolia lectin 1-B(4). X-ray crystal structure of the complex and molecular dynamics characterization of the binding site. J. Biol. Chem. 277:2002;6615-6621.
12. Svensson, C., Teneberg, S., Nilsson, C. L., Kjellberg, A., Schwarz, F. P., Sharon, N., Krengel, U. (2002). High-resolution crystal structures of Erythrina cristagalli lectin in complex with lactose and 2′-alpha-L- fucosyllactose and correlation with thermodynamic binding data. J. Mol. Biol. 321, 69-83.
13. Hamelryck T.W., Loris R., Bouckaert J., Dao-Thi M.H., Strecker G., Imberty A., et al. Carbohydrate binding, quaternary structure and a novel hydrophobic binding site in two legume lectin oligomers from Dolichos biflorus. J. Mol. Biol. 286:1999;1161-1177.
14. Buts L., Dao-Thi M.H., Loris R., Wyns L., Etzler M., Hamelryck T. Weak protein-protein interactions in lectins: the crystal structure of a vegetative lectin from the legume Dolichos biflorus. J. Mol. Biol. 309:2001;193-201.
15. Hamelryck T.W., Moore J.G., Chrispeels M.J., Loris R., Wyns L. The role of weak protein-protein interactions in multivalent lectin-carbohydrate binding: crystal structure of cross-linked FRIL. J. Mol. Biol. 299:2000;875-883.
16. Sanz-Aparicio J., Hermoso J., Grangeiro T.B., Calvete J.J., Cavada B.S. The crystal structure of Canavalia brasiliensis lectin suggests a correlation between its quaternary conformation and its distinct biological properties from concanavalin A. FEBS Letters. 405:1997;114-118.
17. Wah D.A., Romero A., Gallego del Sol F., Cavada B.S., Ramos M.V., Grangeiro T.B., et al. Crystal structure of native and Cd/Cd-substituted Dioclea guianensis seed lectin. A novel manganese-binding site and structural basis of dimer-tetramer association. J. Mol. Biol. 310:2001;885-894.
18. Imberty A., Gautier C., Lescar J., Perez S., Wyns L., Loris R. An unusual carbohydrate binding site revealed by the structures of two Maackia amurensis lectins complexed with sialic acid-containing oligosaccharides. J. Biol. Chem. 275:2000;17541-17548.
19. Loris R., De Greve H., Dao-Thi M.-H., Messens J., Imberty A., Wyns L. Structural basis of carbohydrate recognition by lectin II from Ulex europaeus, a protein with a promiscuous carbohydrate-binding site. J. Mol. Biol. 301:2000;987-1002.
20. Rozwarski D.A., Swami B.M., Brewer C.F., Sacchettini J.C. Crystal structure of the lectin from Dioclea grandiflora complexed with core trimannoside of asparagine-linked carbohydrates. J. Biol. Chem. 273:1998;32818-32825.
21. Nielsen H., Engelbrecht J., Brunak S., von Heijne G. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1997;1-6.
22. Loris R., Imberty A., Beeckmans S., Van Driessche E., Read J.S., Bouckaert J., et al. Crystal structure of Pterocarpus angolensis lectin in complex with glucose, sucrose and turanose. J. Biol. Chem. 278:2003;16297-16303.
23. Chandra N.R., Prabu M.M., Suguna K., Vijayan M. Structural similarity and functional diversity in proteins containing the legume lectin fold. Protein Eng. 14:2001;857-866.
24. Manoj N., Suguna K. Signature of quaternary structure in the sequences of legume lectins. Protein Eng. 14:2001;735-745.
25. Srinivas V.R., Reddy G.B., Ahmad N., Swaminathan C.P., Mitra N., Surolia A. Legume lectin family, the "natural mutants of the quaternary state", provide insights into the relationship between protein stability and oligomerization. Biochim. Biophys. Acta. 1527:2001;102-111.
26. Derewenda Z., Yariv J., Helliwell J.R., Kalb A.J., Dodson E.J., Papiz M.Z., et al. The structure of the saccharide-binding site of concanavalin A. EMBO J. 8:1989;2189-2193.
27. Bourne Y., Roussel A., Frey M., Rouge P., Fontecilla-Camps J.C., Cambillau C. Three-dimensional structures of complexes of Lathyrus ochrus isolectin I with glucose and mannose: fine specificity of the monosaccharide-binding site. Proteins: Struct. Funct. Genet. 8:1990;365-376.
28. Rini J.M., Hardman K.D., Einspahr H., Suddath F.L., Carver J.P. X-ray crystal structure of a pea lectin-trimannoside complex at 2.6 Å resolution. J. Biol. Chem. 268:1993;10126-10132.
29. Delbaere L.T., Vandonselaar M., Prasad L., Quail J.W., Wilson K.S., Dauter Z. Structures of the lectin IV of Griffonia simplicifolia and its complex with the Lewis b human blood group determinant at 2.0 Å resolution. J. Mol. Biol. 230:1993;950-965.
30. Moothoo D.N., Canan B., Field R.A., Naismith J.H. Man(α1-2) Manα-OMe-concanavalin A complex reveals a balance of forces involved in carbohydrate recognition. Glycobiology. 9:1999;539-545.
31. Bouckaert J., Loris R., Hamelryck T., Wyns L. The crystal structures of Man(α1-3)Man and Man(α1-6)Man complexed to concanavalin A. J. Biol. Chem. 274:1999;29188-29195.
32. Brewer C.F., Brown R.D. Mechanism of binding of mono- and oligosaccharides to concanavalin A: a solvent proton magnetic relaxation dispersion study. Biochemistry. 18:1979;2555-2562.
33. Brewer C.F., Bhattacharyya L. Specificity of concanavalin A binding to asparagine-linked glycopeptides. A nuclear magnetic relaxation dispersion study. J. Biol. Chem. 261:1986;7306-7310.
34. Mandal D.K., Kishore N., Brewer C.F. Thermodynamics of lectin-carbohydrate interactions. Titration microcalorimetry measurements of the binding of N-linked carbohydrates and ovalbumin to concanavalin A. Biochemistry. 33:1994;1149-1156.
35. Naismith J.H., Field R.A. Structural basis of trimannoside recognition by concanavalin A. J. Biol. Chem. 271:1996;972-976.
36. Loris R., Maes D., Poortmans F., Wyns L., Bouckaert J. A structure of the complex between concanavalin A and methyl-3,6-di-O-(alpha-D-mannopyranosyl)- alpha-D-mannopyranoside reveals two binding modes. J. Biol. Chem. 271:1996;30614-30618.
37. Frohman M.A. Rapid amplification of complementary DNA ends for generation of full-length complementary DNAs: thermal RACE. Methods Enzymol. 218:1993;340-356.
38. Sanger F., Nicklen S., Coulson A.R. DNA sequencing with chain-terminating inhibitors. Proc. Natl Acad. Sci. USA. 74:1977;5463-5467.
39. Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
40. Loris R., Steyaert J., Maes D., Lisgarten J., Pickersgill R., Wyns L. Crystal structure determination and refinement at 2.3-Å resolution of the lentil lectin. Biochemistry. 32:1993;8772-8781.
41. Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163.
42. Brünger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., et al. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallog. sect. D. 54:1998;905-921.
43. Roussel A., Cambillau C. TURBO-FRODO. Silicon Graphic Geometry Partner Directory. 1989;Silicon Graphics, Mountain View, CA.
44. Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
45. Merritt E.A., Bacon D.J. Raster3D: photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.