1m8n
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(New page: 200px<br /><applet load="1m8n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m8n, resolution 2.45Å" /> '''Choristoneura Fumife...)
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Revision as of 01:49, 25 November 2007
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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
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