2iy9
From Proteopedia
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| - | [[Image:2iy9.gif|left|200px]] | + | [[Image:2iy9.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE A-SUBUNIT OF THE AB5 TOXIN FROM E. COLI''' | + | {{Structure |
| + | |PDB= 2iy9 |SIZE=350|CAPTION= <scene name='initialview01'>2iy9</scene>, resolution 1.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF THE A-SUBUNIT OF THE AB5 TOXIN FROM E. COLI''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2IY9 is a [ | + | 2IY9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IY9 OCA]. |
==Reference== | ==Reference== | ||
| - | AB5 subtilase cytotoxin inactivates the endoplasmic reticulum chaperone BiP., Paton AW, Beddoe T, Thorpe CM, Whisstock JC, Wilce MC, Rossjohn J, Talbot UM, Paton JC, Nature. 2006 Oct 5;443(7111):548-52. PMID:[http:// | + | AB5 subtilase cytotoxin inactivates the endoplasmic reticulum chaperone BiP., Paton AW, Beddoe T, Thorpe CM, Whisstock JC, Wilce MC, Rossjohn J, Talbot UM, Paton JC, Nature. 2006 Oct 5;443(7111):548-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17024087 17024087] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''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 17:34:58 2008'' |
Revision as of 15:34, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE A-SUBUNIT OF THE AB5 TOXIN FROM E. COLI
Overview
AB5 toxins are produced by pathogenic bacteria and consist of enzymatic A subunits that corrupt essential eukaryotic cell functions, and pentameric B subunits that mediate uptake into the target cell. AB5 toxins include the Shiga, cholera and pertussis toxins and a recently discovered fourth family, subtilase cytotoxin, which is produced by certain Shiga toxigenic strains of Escherichia coli. Here we show that the extreme cytotoxicity of this toxin for eukaryotic cells is due to a specific single-site cleavage of the essential endoplasmic reticulum chaperone BiP/GRP78. The A subunit is a subtilase-like serine protease; structural studies revealed an unusually deep active-site cleft, which accounts for its exquisite substrate specificity. A single amino-acid substitution in the BiP target site prevented cleavage, and co-expression of this resistant protein protected transfected cells against the toxin. BiP is a master regulator of endoplasmic reticulum function, and its cleavage by subtilase cytotoxin represents a previously unknown trigger for cell death.
About this Structure
2IY9 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
AB5 subtilase cytotoxin inactivates the endoplasmic reticulum chaperone BiP., Paton AW, Beddoe T, Thorpe CM, Whisstock JC, Wilce MC, Rossjohn J, Talbot UM, Paton JC, Nature. 2006 Oct 5;443(7111):548-52. PMID:17024087
Page seeded by OCA on Thu Mar 20 17:34:58 2008
Categories: Escherichia coli | Single protein | Beddoe, T. | Paton, A W. | Paton, J C. | Rossjohn, J. | Talbot, U M. | Thorpe, C M. | Whisstock, J C. | Wilce, M C.J. | Coli | Plasmid | Shiga | Toxin
