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| [[Image:1m8n.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1m8n| PDB=1m8n | SCENE= }} | | {{STRUCTURE_1m8n| PDB=1m8n | SCENE= }} |
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| '''Choristoneura Fumiferana (Spruce Budworm) Antifreeze Protein Isoform 501'''
| | ===Choristoneura Fumiferana (Spruce Budworm) Antifreeze Protein Isoform 501=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_12105229}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12105229 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12105229}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Antifreeze protein]] | | [[Category: Antifreeze protein]] |
| [[Category: Left-handed beta-helix]] | | [[Category: Left-handed beta-helix]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:46:02 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:26:55 2008'' |
