1EWW

SOLUTION STRUCTURE OF SPRUCE BUDWORM ANTIFREEZE PROTEIN AT 30 DEGREES CELSIUS

Summary for 1EWW

• Entry DOI: 10.2210/pdb1eww/pdb
• Descriptor: ANTIFREEZE PROTEIN (1 entity in total)
• Functional Keywords: beta-helix, antifreeze protein, ice, insect
• Biological source: Choristoneura fumiferana (spruce budworm)
• Total number of polymer chains: 1
• Total formula weight: 9068.03

Authors

Graether, S.P.,Kuiper, M.J.,Gagne, S.M.,Walker, V.K.,Jia, Z.,Sykes, B.D.,Davies, P.L. (deposition date: 2000-04-27, release date: 2000-07-27, Last modification date: 2022-02-16)

Primary citation

Graether, S.P.,Kuiper, M.J.,Gagne, S.M.,Walker, V.K.,Jia, Z.,Sykes, B.D.,Davies, P.L.
Beta-helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect.
Nature, 406:325-328, 2000

PubMed Abstract: 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.

PubMed: 10917537
DOI: 10.1038/35018610

Experimental method

SOLUTION NMR