1l0s
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1l0s |SIZE=350|CAPTION= <scene name='initialview01'>1l0s</scene>, resolution 2.30Å | |PDB= 1l0s |SIZE=350|CAPTION= <scene name='initialview01'>1l0s</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CD:CADMIUM ION'>CD</scene> | + | |LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=TYI:3,5-DIIODOTYROSINE'>TYI</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1eww|1EWW]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l0s OCA], [http://www.ebi.ac.uk/pdbsum/1l0s PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l0s RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Jia, Z.]] | [[Category: Jia, Z.]] | ||
[[Category: Leinala, E K.]] | [[Category: Leinala, E K.]] | ||
| - | [[Category: CD]] | ||
[[Category: antifreeze protein]] | [[Category: antifreeze protein]] | ||
[[Category: iodination]] | [[Category: iodination]] | ||
[[Category: left-handed beta-helix]] | [[Category: left-handed beta-helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:56:25 2008'' |
Revision as of 18:56, 30 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1EWW
| ||||||
| 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
