1L0S

Choristoneura fumiferana (spruce budworm) antifreeze protein isoform 337

Summary for 1L0S

• Entry DOI: 10.2210/pdb1l0s/pdb
• Related: 1EWW
• Descriptor: thermal hysteresis protein, CADMIUM ION (3 entities in total)
• Functional Keywords: left-handed beta-helix, antifreeze protein, iodination
• Biological source: Choristoneura fumiferana (spruce budworm)
• Total number of polymer chains: 4
• Total formula weight: 37440.13

Authors

Leinala, E.K.,Davies, P.L.,Jia, Z. (deposition date: 2002-02-12, release date: 2002-06-19, Last modification date: 2024-11-20)

Primary citation

Leinala, E.K.,Davies, P.L.,Jia, Z.
Crystal structure of beta-helical antifreeze protein points to a general ice binding model.
Structure, 10:619-627, 2002

PubMed Abstract: Reported here is the 2.3 A 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.

PubMed: 12015145
DOI: 10.1016/S0969-2126(02)00745-1

Experimental method

X-RAY DIFFRACTION (2.3 Å)