1eww
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eww OCA], [http://www.ebi.ac.uk/pdbsum/1eww PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eww RCSB]</span> | ||
}} | }} | ||
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[[Category: insect]] | [[Category: insect]] | ||
| - | ''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 20:11:11 2008'' |
Revision as of 17:11, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF SPRUCE BUDWORM ANTIFREEZE PROTEIN AT 30 DEGREES CELSIUS
Overview
Insect antifreeze proteins (AFP) are considerably more active at inhibiting ice crystal growth than AFP from fish or plants. Several insect AFPs, also known as thermal hysteresis proteins, have been cloned and expressed. Their maximum activity is 3-4 times that of fish AFPs and they are 10-100 times more effective at micromolar concentrations. Here we report the solution structure of spruce budworm (Choristoneura fumiferana) AFP and characterize its ice-binding properties. The 9-kDa AFP is a beta-helix with a triangular cross-section and rectangular sides that form stacked parallel beta-sheets; a fold which is distinct from the three known fish AFP structures. The ice-binding side contains 9 of the 14 surface-accessible threonines organized in a regular array of TXT motifs that match the ice lattice on both prism and basal planes. In support of this model, ice crystal morphology and ice-etching experiments are consistent with AFP binding to both of these planes and thus may explain the greater activity of the spruce budworm antifreeze.
About this Structure
1EWW is a Single protein structure of sequence from Choristoneura fumiferana. Full crystallographic information is available from OCA.
Reference
Beta-helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect., Graether SP, Kuiper MJ, Gagne SM, Walker VK, Jia Z, Sykes BD, Davies PL, Nature. 2000 Jul 20;406(6793):325-8. PMID:10917537
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