3ffz
From Proteopedia
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===Domain organization in Clostridium butulinum neurotoxin type E is unique: Its implication in faster translocation=== | ===Domain organization in Clostridium butulinum neurotoxin type E is unique: Its implication in faster translocation=== | ||
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==About this Structure== | ==About this Structure== | ||
3FFZ is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FFZ OCA]. | 3FFZ is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FFZ OCA]. | ||
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| + | ==Reference== | ||
| + | <ref group="xtra">PMID:19118561</ref><references group="xtra"/> | ||
[[Category: Bontoxilysin]] | [[Category: Bontoxilysin]] | ||
[[Category: Clostridium botulinum]] | [[Category: Clostridium botulinum]] | ||
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[[Category: Zinc]] | [[Category: Zinc]] | ||
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Revision as of 06:23, 15 April 2009
Domain organization in Clostridium butulinum neurotoxin type E is unique: Its implication in faster translocation
Template:ABSTRACT PUBMED 19118561
About this Structure
3FFZ is a 2 chains structure of sequences from Clostridium botulinum. Full crystallographic information is available from OCA.
Reference
- Kumaran D, Eswaramoorthy S, Furey W, Navaza J, Sax M, Swaminathan S. Domain organization in Clostridium botulinum neurotoxin type E is unique: its implication in faster translocation. J Mol Biol. 2009 Feb 13;386(1):233-45. Epub 2008 Dec 24. PMID:19118561 doi:10.1016/j.jmb.2008.12.027
Page seeded by OCA on Wed Apr 15 09:23:17 2009
Categories: Bontoxilysin | Clostridium botulinum | Eswaramoorthy, S. | Kumaran, D. | Swaminathan, S. | Botulinum neurotoxin serotype e | Botulism | Domain organization | Endopeptidase | Hydrolase | Membrane | Metal-binding | Metalloprotease | Neurotoxin | Protease | Secreted | Toxin | Translocation | Transmembrane | Zinc
