1l0s
From Proteopedia
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'''Choristoneura fumiferana (spruce budworm) antifreeze protein isoform 337''' | '''Choristoneura fumiferana (spruce budworm) antifreeze protein isoform 337''' | ||
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[[Category: Jia, Z.]] | [[Category: Jia, Z.]] | ||
[[Category: Leinala, E K.]] | [[Category: Leinala, E K.]] | ||
| - | [[Category: | + | [[Category: Antifreeze protein]] |
| - | [[Category: | + | [[Category: Iodination]] |
| - | [[Category: | + | [[Category: Left-handed beta-helix]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:24:46 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 20:24, 2 May 2008
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 Fri May 2 23:24:46 2008
