1qoy

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(New page: 200px<br /><applet load="1qoy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qoy, resolution 2.0&Aring;" /> '''E.COLI HEMOLYSIN E (H...)
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[[Image:1qoy.gif|left|200px]]<br /><applet load="1qoy" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1qoy.gif|left|200px]]<br /><applet load="1qoy" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1qoy, resolution 2.0&Aring;" />
caption="1qoy, resolution 2.0&Aring;" />
'''E.COLI HEMOLYSIN E (HLYE, CLYA, SHEA)'''<br />
'''E.COLI HEMOLYSIN E (HLYE, CLYA, SHEA)'''<br />
==Overview==
==Overview==
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Hemolysin E (HlyE) is a novel pore-forming toxin of Escherichia coli, Salmonella typhi, and Shigella flexneri. Here we report the X-ray crystal, structure of the water-soluble form of E. coli HlyE at 2.0 A resolution, and the visualization of the lipid-associated form of the toxin in, projection at low resolution by electron microscopy. The crystal structure, reveals HlyE to be the first member of a new family of toxin structures, consisting of an elaborated helical bundle some 100 A long. The electron, micrographs show how HlyE oligomerizes in the presence of lipid to form, transmembrane pores. Taken together, the data from these two structural, techniques allow us to propose a simple model for the structure of the, pore and for membrane interaction.
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Hemolysin E (HlyE) is a novel pore-forming toxin of Escherichia coli, Salmonella typhi, and Shigella flexneri. Here we report the X-ray crystal structure of the water-soluble form of E. coli HlyE at 2.0 A resolution and the visualization of the lipid-associated form of the toxin in projection at low resolution by electron microscopy. The crystal structure reveals HlyE to be the first member of a new family of toxin structures, consisting of an elaborated helical bundle some 100 A long. The electron micrographs show how HlyE oligomerizes in the presence of lipid to form transmembrane pores. Taken together, the data from these two structural techniques allow us to propose a simple model for the structure of the pore and for membrane interaction.
==About this Structure==
==About this Structure==
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1QOY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QOY OCA].
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1QOY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOY OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Artymiuk, P.J.]]
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[[Category: Artymiuk, P J.]]
[[Category: Atkins, A.]]
[[Category: Atkins, A.]]
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[[Category: Bullough, P.A.]]
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[[Category: Bullough, P A.]]
[[Category: Green, J.]]
[[Category: Green, J.]]
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[[Category: Jamieson, S.J.]]
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[[Category: Jamieson, S J.]]
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[[Category: Stillman, T.J.]]
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[[Category: Stillman, T J.]]
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[[Category: Wallace, A.J.]]
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[[Category: Wallace, A J.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: cytolysin]]
[[Category: cytolysin]]
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[[Category: toxin]]
[[Category: toxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:51:21 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:42:05 2008''

Revision as of 12:42, 21 February 2008


1qoy, resolution 2.0Å

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E.COLI HEMOLYSIN E (HLYE, CLYA, SHEA)

Overview

Hemolysin E (HlyE) is a novel pore-forming toxin of Escherichia coli, Salmonella typhi, and Shigella flexneri. Here we report the X-ray crystal structure of the water-soluble form of E. coli HlyE at 2.0 A resolution and the visualization of the lipid-associated form of the toxin in projection at low resolution by electron microscopy. The crystal structure reveals HlyE to be the first member of a new family of toxin structures, consisting of an elaborated helical bundle some 100 A long. The electron micrographs show how HlyE oligomerizes in the presence of lipid to form transmembrane pores. Taken together, the data from these two structural techniques allow us to propose a simple model for the structure of the pore and for membrane interaction.

About this Structure

1QOY is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

Reference

E. coli hemolysin E (HlyE, ClyA, SheA): X-ray crystal structure of the toxin and observation of membrane pores by electron microscopy., Wallace AJ, Stillman TJ, Atkins A, Jamieson SJ, Bullough PA, Green J, Artymiuk PJ, Cell. 2000 Jan 21;100(2):265-76. PMID:10660049

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