1z0h
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.69 3.4.24.69] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.69 3.4.24.69] </span> |
|GENE= botB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1491 Clostridium botulinum]) | |GENE= botB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1491 Clostridium botulinum]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1erw|1ERW]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z0h OCA], [http://www.ebi.ac.uk/pdbsum/1z0h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1z0h RCSB]</span> | ||
}} | }} | ||
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[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:27:15 2008'' |
Revision as of 22:27, 30 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | botB (Clostridium botulinum) | ||||||
| Activity: | Bontoxilysin, with EC number 3.4.24.69 | ||||||
| Related: | 1ERW
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B
Overview
Botulinum neurotoxins comprise seven distinct serotypes (A-G) produced by Clostridium botulinum. The crystal structure of the binding domain of the botulinum neurotoxin type B (BBHc) has been determined to 2A resolution. The overall structure of BBHc is well ordered and similar to that of the binding domain of the holotoxin. However, significant structural changes occur at what would be the interface of translocation and binding domains of the holotoxin. The loop 911-924 shows a maximum displacement of 14.8A at the farthest point. The N-terminal helix reorients and moves by 19.5A from its original position. BBHc is compared with the binding domain of the holotoxin of botulinum type A and B, and the tetanus C-fragment to characterize the heavy chain-carbohydrate interactions. The probable reasons for different binding affinity of botulinum and tetanus toxins are discussed.
About this Structure
1Z0H is a Single protein structure of sequence from Clostridium botulinum. Full crystallographic information is available from OCA.
Reference
N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B., Jayaraman S, Eswaramoorthy S, Ahmed SA, Smith LA, Swaminathan S, Biochem Biophys Res Commun. 2005 Apr 29;330(1):97-103. PMID:15781237
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