Figure 3 - full size

 

Figure 3.
Crystal structures show canonical dimer interface and destabilized loops. a, superposition of κI O18/O8 (blue) and AL-09 H87Y (orange) shows restored dimer interface. b, differences in the loop between Lys-39 and Pro-44 are visible in the global superposition of κI O18/O8 (blue) and κI O18/O8 Y87H (red). c, superposition of κI O18/O8 (blue) and κI O18/O8 N34I/Y87H (green) shows a change in the same loop as observed in b. d, shift of Pro-40 and Gly-41 in the κI O18/O8 Y87H mutant (pink) disrupts an interaction between Tyr-87 and the carbonyl of Gly-41. e, detailed view of Pro-40 and Gly-41 of κI O18/O8 (blue) and κI O18/O8 N34I/Y87H (green) shows same disrupted interaction as observed with the κI O18/O8 Y87H mutant in d. f, hydrogen bonding between the backbone carbonyl of Lys-42 and the OH of Tyr-87 in κI O18/O8 (blue) is lacking with the His-87 mutation in κI O18/O8 Y87H (pink). This is also observed in the κI O18/O8 N34I/Y87H mutant (not pictured).

The above figure is reprinted from an Open Access publication published by the ASBMB: J Biol Chem (2008, 283, 30950-30956) copyright 2008.