1l0s

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(New page: 200px<br /><applet load="1l0s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l0s, resolution 2.30&Aring;" /> '''Choristoneura fumife...)
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Revision as of 00:09, 25 November 2007

Image:1l0s.jpg

1l0s, resolution 2.30Å

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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 with CD as ligand. 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

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