A Variety of Saccharide Binding-Sites
- 560 Downloads
This chapter is devoted to discussion of protein binding–sites for saccharides for two main reasons. One is sentimental and self-serving and deals with J.B. Sumner who accidentally isolated concanavalin A when he proved in the twenties of the last century that enzymes are proteins (reference to Sumner is in Chap. 1). Concanavalin A is a protein where this author can mention his own contribution to the understanding of its structure and, in particular, its binding site for glucose and mannose. The other reason is lac-operon repressor that played such a crucial role in molecular biology and eventually provided a description in atomic detail of its interaction with DNA. A short summary of saccharide structure and nomenclature introduces this chapter. It describes as well a cellulose-binding protein that facilitates hydrolysis of crystalline cellulose by cellulases.
KeywordsIdentical Monomer Repressor Molecule Met84 Mutant Protein Heat Stability Residue Form Hydrogen Bond
- Brewer CF, Sternlicht H, Marcus DM, Grollman AP (1973) Interaction of saccharides with concanavalin A. Mechanism of binding of α- and β-methyl D-glucopyranoside to concanavalin a as determined by13C nuclear magnetic resonance. Biochemistry 12:4448–4457Google Scholar
- Gosh M, Meerts IATM, Cook A, Bergman A, Brouwer A, Johnson LN (2000) Structure of human transthyrethin complexed with bromophenols: a new mode of binding. Acta Crystallogr D Biol Crystallogr D56:2189–2193Google Scholar
- Naismith JH, Emmerich C, Habash J, Harrop SJ, Helliwell JR, Hunter WN, Raftery J, Kalb(Gilboa) AJ, Yariv J (1994) Refined structure of concanavalin a complexed with methyl α-D-mannopyranoside at 2 Å resolution and comparison with saccharide-free structure. Acta Crystallogr D Biol Crystallogr D50:847–858Google Scholar
- Yariv J, Kalb(Gilboa) AJ, Papiz MZ, Helliwell JR, Andrews SJ, Habash J (1987) Properties of a new crystal form of the complex of concanavalin a with methyl α-D-glucopyranoside. J Mol Biol 195:759–760Google Scholar