1l0s
From Proteopedia
(New page: 200px<br /><applet load="1l0s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l0s, resolution 2.30Å" /> '''Choristoneura fumife...) |
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- | [[Image:1l0s.jpg|left|200px]]<br /><applet load="1l0s" size=" | + | [[Image:1l0s.jpg|left|200px]]<br /><applet load="1l0s" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1l0s, resolution 2.30Å" /> | caption="1l0s, resolution 2.30Å" /> | ||
'''Choristoneura fumiferana (spruce budworm) antifreeze protein isoform 337'''<br /> | '''Choristoneura fumiferana (spruce budworm) antifreeze protein isoform 337'''<br /> | ||
==Overview== | ==Overview== | ||
- | Reported here is the 2.3 A resolution crystal structure of spruce budworm | + | Reported here is the 2.3 A resolution crystal structure of spruce budworm (Choristoneura fumiferana) antifreeze protein (CfAFP), solved by single anomalous scattering. The structure reveals an extremely regular left-handed beta-helical platform consisting of 15-amino acid loops with a repetitive Thr-X-Thr motif displayed on one of the helix's three faces. This motif results in a two-dimensional array of threonine residues in an identical orientation to those in the nonhomologous, right-handed beta-helical beetle AFP from Tenebrio molitor (TmAFP). The CfAFP structure led us to reevaluate our ice binding model, and the analysis of three possible modes of docking gives rise to a binding mechanism based on surface complementarity. This general mechanism is applicable to both fish and insect AFPs. |
==About this Structure== | ==About this Structure== | ||
- | 1L0S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Choristoneura_fumiferana Choristoneura fumiferana] with CD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1L0S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Choristoneura_fumiferana Choristoneura fumiferana] with <scene name='pdbligand=CD:'>CD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L0S OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Choristoneura fumiferana]] | [[Category: Choristoneura fumiferana]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
- | [[Category: Davies, P | + | [[Category: Davies, P L.]] |
[[Category: Jia, Z.]] | [[Category: Jia, Z.]] | ||
- | [[Category: Leinala, E | + | [[Category: Leinala, E K.]] |
[[Category: CD]] | [[Category: CD]] | ||
[[Category: antifreeze protein]] | [[Category: antifreeze protein]] | ||
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[[Category: left-handed beta-helix]] | [[Category: left-handed beta-helix]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:04 2008'' |
Revision as of 11:40, 21 February 2008
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Choristoneura fumiferana (spruce budworm) antifreeze protein isoform 337
Overview
Reported here is the 2.3 A resolution crystal structure of spruce budworm (Choristoneura fumiferana) antifreeze protein (CfAFP), solved by single anomalous scattering. The structure reveals an extremely regular left-handed beta-helical platform consisting of 15-amino acid loops with a repetitive Thr-X-Thr motif displayed on one of the helix's three faces. This motif results in a two-dimensional array of threonine residues in an identical orientation to those in the nonhomologous, right-handed beta-helical beetle AFP from Tenebrio molitor (TmAFP). The CfAFP structure led us to reevaluate our ice binding model, and the analysis of three possible modes of docking gives rise to a binding mechanism based on surface complementarity. This general mechanism is applicable to both fish and insect AFPs.
About this Structure
1L0S is a Single protein structure of sequence from Choristoneura fumiferana with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of beta-helical antifreeze protein points to a general ice binding model., Leinala EK, Davies PL, Jia Z, Structure. 2002 May;10(5):619-27. PMID:12015145
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