1m8n: Difference between revisions
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'''Choristoneura Fumiferana (Spruce Budworm) Antifreeze Protein Isoform 501''' | {{Structure | ||
|PDB= 1m8n |SIZE=350|CAPTION= <scene name='initialview01'>1m8n</scene>, resolution 2.45Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Choristoneura Fumiferana (Spruce Budworm) Antifreeze Protein Isoform 501''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1M8N is a [ | 1M8N is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Choristoneura_fumiferana Choristoneura fumiferana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M8N OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12105229 12105229] | ||
[[Category: Choristoneura fumiferana]] | [[Category: Choristoneura fumiferana]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: left-handed beta-helix]] | [[Category: left-handed beta-helix]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:40:20 2008'' | ||
Revision as of 10:40, 20 March 2008
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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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