Journal
STRUCTURE
Volume 10, Issue 5, Pages 619-627Publisher
CELL PRESS
DOI: 10.1016/S0969-2126(02)00745-1
Keywords
antifreeze protein; beta helix; ice binding; surface complementarity; X-ray structure; single anomalous scattering
Ask authors/readers for more resources
Reported here is the 2.3 Angstrom resolution crystal structure of spruce budworm (Choristoneura fumiferana) antifreeze protein (CfAFP), solved by single anomalous scattering. The structure reveals an extremely regular left-handed beta-helical platform consisting of 15-amino acid loops with a repetitive Thr-X-Thr motif displayed on one of the helix's three faces. This motif results in a two-dimensional array of threonine residues in an identical orientation to those in the nonhomologous, right-handed beta-helical beetle AFP from Tenebrio molitor (TmAFP). The CfAFP structure led us to reevaluate our ice binding model, and the analysis of three possible modes of docking gives rise to a binding mechanism based on surface complementarity. This general mechanism is applicable to both fish and insect AFPs.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available