1l0s

Choristoneura fumiferana (spruce budworm) antifreeze protein isoform 337

spinqualitylabelsall models 1l0s, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1l0s is a 4 chain structure with sequence from Choristoneura fumiferana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: CD, TYI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9GTP0_CHOFU Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Antifreeze protein 3D structures

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