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1l0s
From Proteopedia
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| , resolution 2.30Å | |||||||
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| Ligands: | , | ||||||
| Related: | 1EWW
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Choristoneura fumiferana (spruce budworm) antifreeze protein isoform 337
Overview
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.
About this Structure
1L0S is a Single protein structure of sequence from Choristoneura fumiferana. Full crystallographic information is available from OCA.
Reference
Crystal structure of beta-helical antifreeze protein points to a general ice binding model., Leinala EK, Davies PL, Jia Z, Structure. 2002 May;10(5):619-27. PMID:12015145
Page seeded by OCA on Sun Mar 30 21:56:25 2008
