1m8n

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[[Image:1m8n.gif|left|200px]]
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{{Structure
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|RELATEDENTRY=[[1l0s|1L0S]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m8n OCA], [http://www.ebi.ac.uk/pdbsum/1m8n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m8n RCSB]</span>
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'''Choristoneura Fumiferana (Spruce Budworm) Antifreeze Protein Isoform 501'''
'''Choristoneura Fumiferana (Spruce Budworm) Antifreeze Protein Isoform 501'''
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[[Category: Jia, Z.]]
[[Category: Jia, Z.]]
[[Category: Leinala, E K.]]
[[Category: Leinala, E K.]]
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[[Category: antifreeze protein,]]
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[[Category: Antifreeze protein]]
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[[Category: left-handed beta-helix]]
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[[Category: Left-handed beta-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:46:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:12:55 2008''
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Revision as of 21:46, 2 May 2008

Template:STRUCTURE 1m8n

Choristoneura Fumiferana (Spruce Budworm) Antifreeze Protein Isoform 501


Overview

The insect spruce budworm (Choristoneura fumiferana)(Cf) produces a number of isoforms of its highly active antifreeze protein (CfAFP). Although most of the CfAFP isoforms are in the 9-kDa range, isoforms containing a 30- or 31-amino acid insertion have also been identified. Here we describe the functional and structural analysis of a selected long isoform, CfAFP-501. X-ray crystal structure determination reveals that the 31-amino acid insertion found in CfAFP-501 forms two additional loops within its highly regular beta-helical structure. This effectively extends the area of the two-dimensional Thr array and ice-binding surface of the protein. The larger isoform has 3 times the thermal hysteresis activity of the 9-kDa CfAFP-337. As well, a deletion of the 31-amino acid insertion within CfAFP-501 to form CfAFP-501-Delta-2-loop, results in a protein with reduced activity similar to the shorter CfAFP isoforms. Thus, the enhanced antifreeze activity of CfAFP-501 is directly correlated to the length of its beta-helical structure and hence the size of its ice-binding face.

About this Structure

1M8N is a Single protein structure of sequence from Choristoneura fumiferana. Full crystallographic information is available from OCA.

Reference

A beta-helical antifreeze protein isoform with increased activity. Structural and functional insights., Leinala EK, Davies PL, Doucet D, Tyshenko MG, Walker VK, Jia Z, J Biol Chem. 2002 Sep 6;277(36):33349-52. Epub 2002 Jun 24. PMID:12105229 Page seeded by OCA on Sat May 3 00:46:02 2008

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