1n4i

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[[Image:1n4i.jpg|left|200px]]
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{{Structure
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{{STRUCTURE_1n4i| PDB=1n4i | SCENE= }}
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|RELATEDENTRY=[[1eww|1EWW]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n4i OCA], [http://www.ebi.ac.uk/pdbsum/1n4i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1n4i RCSB]</span>
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'''Solution structure of spruce budworm antifreeze protein at 5 degrees celsius'''
'''Solution structure of spruce budworm antifreeze protein at 5 degrees celsius'''
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[[Category: Spyracopoulos, L.]]
[[Category: Spyracopoulos, L.]]
[[Category: Sykes, B D.]]
[[Category: Sykes, B D.]]
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[[Category: antifreeze protein]]
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[[Category: Antifreeze protein]]
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[[Category: beta-helix]]
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[[Category: Beta-helix]]
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[[Category: ice]]
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[[Category: Ice]]
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[[Category: insect]]
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[[Category: Insect]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:05:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:25:22 2008''
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Revision as of 23:05, 2 May 2008

Template:STRUCTURE 1n4i

Solution structure of spruce budworm antifreeze protein at 5 degrees celsius


Overview

Antifreeze proteins (AFPs) prevent the growth of ice, and are used by some organisms that live in sub-zero environments for protection against freezing. All AFPs are thought to function by an adsorption inhibition process. In order to elucidate the ice-binding mechanism, the structures of several AFPs have been determined, and have been shown to consist of different folds. Recently, the first structures of the highly active insect AFPs have been characterized. These proteins have a beta-helix structure, which adds yet another fold to the AFP family. The 90-residue spruce budworm (Choristoneura fumiferana) AFP consists of a beta-helix with 15 residues per coil. The structure contains two ranks of aligned threonine residues (known as the TXT motif), which were shown by mutagenesis experiments to be located in the ice-binding face. In our previous NMR study of this AFP at 30 degrees C, we found that the TXT face was not optimally defined because of the broadening of NMR resonances potentially due to weak oligomerization. We present here a structure of spruce budworm AFP determined at 5 degrees C, where this broadening is reduced. In addition, the 1H-15N NMR dynamics of the protein were examined at 30 degrees C and 5 degrees C. The results show that the spruce budworm AFP is more structured at 5 degrees C, and support the general observation that AFPs become more rigid as the temperature is lowered.

About this Structure

1N4I is a Single protein structure of sequence from Choristoneura fumiferana. Full crystallographic information is available from OCA.

Reference

Spruce budworm antifreeze protein: changes in structure and dynamics at low temperature., Graether SP, Gagne SM, Spyracopoulos L, Jia Z, Davies PL, Sykes BD, J Mol Biol. 2003 Apr 11;327(5):1155-68. PMID:12662938 Page seeded by OCA on Sat May 3 02:05:06 2008

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