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EMBO J. May 4, 1999; 18(9): 2313–2322.
PMCID: PMC1171314

Tachylectin-2: crystal structure of a specific GlcNAc/GalNAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus.

Abstract

Tachylectin-2, isolated from large granules of the hemocytes of the Japanese horseshoe crab (Tachypleus tridentatus), is a 236 amino acid protein belonging to the lectins. It binds specifically to N-acetylglucosamine and N-acetylgalactosamine and is a part of the innate immunity host defense system of the horseshoe crab. The X-ray structure of tachylectin-2 was solved at 2.0 A resolution by the multiple isomorphous replacement method and this molecular model was employed to solve the X-ray structure of the complex with N-acetylglucosamine. Tachylectin-2 is the first protein displaying a five-bladed beta-propeller structure. Five four-stranded antiparallel beta-sheets of W-like topology are arranged around a central water-filled tunnel, with the water molecules arranged as a pentagonal dodecahedron. Tachylectin-2 exhibits five virtually identical binding sites, one in each beta-sheet. The binding sites are located between adjacent beta-sheets and are made by a large loop between the outermost strands of the beta-sheets and the connecting segment from the previous beta-sheet. The high number of five binding sites within the single polypeptide chain strongly suggests the recognition of carbohydrate surface structures of pathogens with a fairly high ligand density. Thus, tachylectin-2 employs strict specificity for certain N-acetyl sugars as well as the surface ligand density for self/non-self recognition.

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Selected References

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  • Abrahams JP, Leslie AG. Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):30–42. [PubMed]
  • Baker SC, Saunders NF, Willis AC, Ferguson SJ, Hajdu J, Fülöp V. Cytochrome cd1 structure: unusual haem environments in a nitrite reductase and analysis of factors contributing to beta-propeller folds. J Mol Biol. 1997 Jun 13;269(3):440–455. [PubMed]
  • Bergner A, Oganessyan V, Muta T, Iwanaga S, Typke D, Huber R, Bode W. Crystal structure of a coagulogen, the clotting protein from horseshoe crab: a structural homologue of nerve growth factor. EMBO J. 1996 Dec 16;15(24):6789–6797. [PMC free article] [PubMed]
  • Brünger AT, Kuriyan J, Karplus M. Crystallographic R factor refinement by molecular dynamics. Science. 1987 Jan 23;235(4787):458–460. [PubMed]
  • Burrows L, Iobst ST, Drickamer K. Selective binding of N-acetylglucosamine to the chicken hepatic lectin. Biochem J. 1997 Jun 1;324(Pt 2):673–680. [PMC free article] [PubMed]
  • Faber HR, Groom CR, Baker HM, Morgan WT, Smith A, Baker EN. 1.8 A crystal structure of the C-terminal domain of rabbit serum haemopexin. Structure. 1995 Jun 15;3(6):551–559. [PubMed]
  • Fearon DT, Locksley RM. The instructive role of innate immunity in the acquired immune response. Science. 1996 Apr 5;272(5258):50–53. [PubMed]
  • Inamori K, Saito T, Iwaki D, Nagira T, Iwanaga S, Arisaka F, Kawabata S. A newly identified horseshoe crab lectin with specificity for blood group A antigen recognizes specific O-antigens of bacterial lipopolysaccharides. J Biol Chem. 1999 Feb 5;274(6):3272–3278. [PubMed]
  • Ito N, Phillips SE, Stevens C, Ogel ZB, McPherson MJ, Keen JN, Yadav KD, Knowles PF. Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase. Nature. 1991 Mar 7;350(6313):87–90. [PubMed]
  • Iwanaga S, Kawabata S, Muta T. New types of clotting factors and defense molecules found in horseshoe crab hemolymph: their structures and functions. J Biochem. 1998 Jan;123(1):1–15. [PubMed]
  • Lamzin VS, Wilson KS. Automated refinement of protein models. Acta Crystallogr D Biol Crystallogr. 1993 Jan 1;49(Pt 1):129–147. [PubMed]
  • Li J, Brick P, O'Hare MC, Skarzynski T, Lloyd LF, Curry VA, Clark IM, Bigg HF, Hazleman BL, Cawston TE, et al. Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed beta-propeller. Structure. 1995 Jun 15;3(6):541–549. [PubMed]
  • Matthews BW. Solvent content of protein crystals. J Mol Biol. 1968 Apr 28;33(2):491–497. [PubMed]
  • Medzhitov R, Janeway CA., Jr Innate immunity: the virtues of a nonclonal system of recognition. Cell. 1997 Oct 31;91(3):295–298. [PubMed]
  • Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):240–255. [PubMed]
  • Murzin AG. Structural principles for the propeller assembly of beta-sheets: the preference for seven-fold symmetry. Proteins. 1992 Oct;14(2):191–201. [PubMed]
  • Muta T, Seki N, Takaki Y, Hashimoto R, Oda T, Iwanaga A, Tokunaga F, Iwanaga S. Purified horseshoe crab factor G. Reconstitution and characterization of the (1-->3)-beta-D-glucan-sensitive serine protease cascade. J Biol Chem. 1995 Jan 13;270(2):892–897. [PubMed]
  • Nakamura S, Iwanaga S, Harada T, Niwa M. A clottable protein (coagulogen) from amoebocyte lysate of Japanese horseshoe crab (Tachypleus tridentatus). Its isolation and biochemical properties. J Biochem. 1976 Nov;80(5):1011–1021. [PubMed]
  • Nakamura T, Tokunaga F, Morita T, Iwanaga S, Kusumoto S, Shiba T, Kobayashi T, Inoue K. Intracellular serine-protease zymogen, factor C, from horseshoe crab hemocytes. Its activation by synthetic lipid A analogues and acidic phospholipids. Eur J Biochem. 1988 Sep 1;176(1):89–94. [PubMed]
  • Nicholls A, Sharp KA, Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins. 1991;11(4):281–296. [PubMed]
  • Okino N, Kawabata S, Saito T, Hirata M, Takagi T, Iwanaga S. Purification, characterization, and cDNA cloning of a 27-kDa lectin (L10) from horseshoe crab hemocytes. J Biol Chem. 1995 Dec 29;270(52):31008–31015. [PubMed]
  • Ruhland GJ, Fiedler F. Occurrence and structure of lipoteichoic acids in the genus Staphylococcus. Arch Microbiol. 1990;154(4):375–379. [PubMed]
  • Saito T, Kawabata S, Hirata M, Iwanaga S. A novel type of limulus lectin-L6. Purification, primary structure, and antibacterial activity. J Biol Chem. 1995 Jun 16;270(24):14493–14499. [PubMed]
  • Saito T, Hatada M, Iwanaga S, Kawabata S. A newly identified horseshoe crab lectin with binding specificity to O-antigen of bacterial lipopolysaccharides. J Biol Chem. 1997 Dec 5;272(49):30703–30708. [PubMed]
  • Tanaka S, Iwanaga S. Limulus test for detecting bacterial endotoxins. Methods Enzymol. 1993;223:358–364. [PubMed]
  • Turner MW. Mannose-binding lectin: the pluripotent molecule of the innate immune system. Immunol Today. 1996 Nov;17(11):532–540. [PubMed]
  • Weis W, Brown JH, Cusack S, Paulson JC, Skehel JJ, Wiley DC. Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature. 1988 Jun 2;333(6172):426–431. [PubMed]
  • Weis WI, Drickamer K. Trimeric structure of a C-type mannose-binding protein. Structure. 1994 Dec 15;2(12):1227–1240. [PubMed]
  • Weis WI, Drickamer K. Structural basis of lectin-carbohydrate recognition. Annu Rev Biochem. 1996;65:441–473. [PubMed]
  • Wright CS. 2.2 A resolution structure analysis of two refined N-acetylneuraminyl-lactose--wheat germ agglutinin isolectin complexes. J Mol Biol. 1990 Oct 20;215(4):635–651. [PubMed]
  • Xia ZX, Dai WW, Xiong JP, Hao ZP, Davidson VL, White S, Mathews FS. The three-dimensional structures of methanol dehydrogenase from two methylotrophic bacteria at 2.6-A resolution. J Biol Chem. 1992 Nov 5;267(31):22289–22297. [PubMed]

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