Arabinose-binding protein structure

Figure 4.21 The polypeptide chain of the arabinose-binding protein in E. coli contains two open twisted a/P domains of similar structure. A schematic diagram of one of these domains is shown in (a). The two domains are oriented such that the carboxy ends of the parallel P strands face each other on opposite sides of a crevice in which the sugar molecule binds, as illustrated in the topology diagram (b). [(a) Adapted from J. Richardson.)...

Most of the information on interdomain motions come from high-resolution crystal structures several reviews are available (Janin and Wodak 1983 Bennett andHuber 1984 Gerstein et al. 1994). Calculations ofhinge bending modes and domain motions in proteins other than lysozyme have been made. They include antibody molecules where the interdomain motions occur on a nanosecond time scale (McCammon and Karplus 1977 Oi et al. 1984), 1-arabinose-binding protein (Mao et al. 1982), liver alcohol dehydrogenase (Colona-Cesari et al. 1986) and the mouse... 

Gilliland, G. L. and Quiocho, F. Q. (1981) Structure of the L-Arabinose-binding Protein From Escherichia coliat2.4 A Resolution,/. Mol. Biol. 146,341-362. 

These principles are well illustrated by the 1.1-k analysis of the L-arabinose complex with L-arabinose-binding protein shown in Fig. 2 44). The extensively refined structure is the most detailed example of a hydrogen bond network at a... 

Fio. 2. Schematic representation from the extensively refined structure analysis of L-arabinose complexed with the L-arabinose-binding protein. Two levels of hydrogen bonds stabilizing the structure are shown. The residues in shell I hydrogen bond to L-arabinose and to shell II. Adapted horn Quiocho and Vyas (44) with permission from Nature. 

Fig. 1 Crystal structures of the periplasmic L-arabinose-binding protein (ABP) of Escherichia coli complexed to a-L-arabinose (left. PDB entry lABE) and of galectin-1 complexed to A-acetyllactosamine (right, PDB entry ISLT). (From Refs. [13-15]). (View this art in color at www.dekker.com.)...

The L-arabinose-binding protein from Escherichia coli also shows two domains with a cleft between them. Quiocho et in this case too, comment on the similarities between the secondary-structural features of these domains, each... 

Structural changes in the protein accompany binding, as indicated by the inaccessibility of the bound L-arabinose to the aqueous environment [19]. Interestingly, unlike many other carbohydrate binding proteins that display a strict anomeric selectivity, a-L-arabinose can be equally well accommodated in the carbohydrate-binding site of this protein. In this case, however, only... 

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