1l0s

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(New page: 200px<br /><applet load="1l0s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l0s, resolution 2.30&Aring;" /> '''Choristoneura fumife...)
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[[Image:1l0s.jpg|left|200px]]<br /><applet load="1l0s" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1l0s.jpg|left|200px]]<br /><applet load="1l0s" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1l0s, resolution 2.30&Aring;" />
caption="1l0s, resolution 2.30&Aring;" />
'''Choristoneura fumiferana (spruce budworm) antifreeze protein isoform 337'''<br />
'''Choristoneura fumiferana (spruce budworm) antifreeze protein isoform 337'''<br />
==Overview==
==Overview==
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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.
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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L0S OCA].
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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]]
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[[Category: Davies, P.L.]]
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[[Category: Davies, P L.]]
[[Category: Jia, Z.]]
[[Category: Jia, Z.]]
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[[Category: Leinala, E.K.]]
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[[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]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:16:54 2007''
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''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


1l0s, resolution 2.30Å

Drag the structure with the mouse to rotate

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

Page seeded by OCA on Thu Feb 21 13:40:04 2008

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