Figure 7 - full size

 

Figure 7.
Figure 7. The site of the disulfide bond of 70--92. A, Superposition of chain C of 70--92 on chain C of wild- type (red). There are two different conformations of mutant observed, type I (yellow) and type II (green) (Table 5). These differ in the conformation of the disulfide bond. B, Superposition of chain C of 70--92, type I only (yellow), on chain C of wild-type (red), some side- chain N atoms are shown in blue. The salt-bridge between Arg 69 and Asp 93 in wild-type is disrupted in the mutant. In the mutant crystal structure the side-chain is solvated and incompletely defined. In the mutant the side-chain of Lys66 occupies the cavity left by Arg69, but no hydrogen bonds are formed with Asp93.

The above figure is reprinted by permission from Elsevier: J Mol Biol (1995, 253, 493-504) copyright 1995.