1m24

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(New page: 200px<br /><applet load="1m24" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m24, resolution 0.90&Aring;" /> '''Trichotoxin_A50E, An...)
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[[Image:1m24.jpg|left|200px]]<br /><applet load="1m24" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1m24, resolution 0.90&Aring;" />
caption="1m24, resolution 0.90&Aring;" />
'''Trichotoxin_A50E, An Ion Channel-Forming Polypeptide'''<br />
'''Trichotoxin_A50E, An Ion Channel-Forming Polypeptide'''<br />
==Overview==
==Overview==
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Trichotoxin_A50E is an 18-residue peptaibol antibiotic which forms, multimeric transmembrane channels through self-association. The crystal, structure of trichotoxin has been determined at a resolution of 0.9 A. The, trichotoxin sequence contains nine helix-promoting Aib residues, which, contribute to the formation of an entirely helical structure that has a, central bend of 8-10 degrees located between residues 10-13. Trichotoxin, is the first solved structure of the peptaibol family that is all, alpha-helix as opposed to containing part or all 3(10)-helix. Gln residues, in positions 6 and 17 produce a polar face, and are proposed to form the, channel lumen. An octameric model channel has been constructed from the, crystal structure. It has a central pore of approximately 4-5 A radius, a, size sufficient to enable transport of ions, with a constricted region at, one end, formed by a ring of Gln6 residues. Electrostatic calculations are, consistent with it being a cationic channel.
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Trichotoxin_A50E is an 18-residue peptaibol antibiotic which forms multimeric transmembrane channels through self-association. The crystal structure of trichotoxin has been determined at a resolution of 0.9 A. The trichotoxin sequence contains nine helix-promoting Aib residues, which contribute to the formation of an entirely helical structure that has a central bend of 8-10 degrees located between residues 10-13. Trichotoxin is the first solved structure of the peptaibol family that is all alpha-helix as opposed to containing part or all 3(10)-helix. Gln residues in positions 6 and 17 produce a polar face, and are proposed to form the channel lumen. An octameric model channel has been constructed from the crystal structure. It has a central pore of approximately 4-5 A radius, a size sufficient to enable transport of ions, with a constricted region at one end, formed by a ring of Gln6 residues. Electrostatic calculations are consistent with it being a cationic channel.
==About this Structure==
==About this Structure==
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1M24 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Trichoderma_viride Trichoderma viride] with ACE and CCN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M24 OCA].
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1M24 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Trichoderma_viride Trichoderma viride] with <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=CCN:'>CCN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M24 OCA].
==Reference==
==Reference==
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[[Category: Trichoderma viride]]
[[Category: Trichoderma viride]]
[[Category: Brueckner, H.]]
[[Category: Brueckner, H.]]
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[[Category: Chugh, J.K.]]
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[[Category: Chugh, J K.]]
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[[Category: Wallace, B.A.]]
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[[Category: Wallace, B A.]]
[[Category: ACE]]
[[Category: ACE]]
[[Category: CCN]]
[[Category: CCN]]
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[[Category: peptaibol]]
[[Category: peptaibol]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:40:50 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:41 2008''

Revision as of 11:50, 21 February 2008


1m24, resolution 0.90Å

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Trichotoxin_A50E, An Ion Channel-Forming Polypeptide

Overview

Trichotoxin_A50E is an 18-residue peptaibol antibiotic which forms multimeric transmembrane channels through self-association. The crystal structure of trichotoxin has been determined at a resolution of 0.9 A. The trichotoxin sequence contains nine helix-promoting Aib residues, which contribute to the formation of an entirely helical structure that has a central bend of 8-10 degrees located between residues 10-13. Trichotoxin is the first solved structure of the peptaibol family that is all alpha-helix as opposed to containing part or all 3(10)-helix. Gln residues in positions 6 and 17 produce a polar face, and are proposed to form the channel lumen. An octameric model channel has been constructed from the crystal structure. It has a central pore of approximately 4-5 A radius, a size sufficient to enable transport of ions, with a constricted region at one end, formed by a ring of Gln6 residues. Electrostatic calculations are consistent with it being a cationic channel.

About this Structure

1M24 is a Protein complex structure of sequences from Trichoderma viride with and as ligands. Full crystallographic information is available from OCA.

Reference

Model for a helical bundle channel based on the high-resolution crystal structure of trichotoxin_A50E., Chugh JK, Bruckner H, Wallace BA, Biochemistry. 2002 Oct 29;41(43):12934-41. PMID:12390019

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