1z0h: Difference between revisions

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[[Image:1z0h.gif|left|200px]]<br /><applet load="1z0h" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1z0h.gif|left|200px]]
caption="1z0h, resolution 2.00&Aring;" />
 
'''N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B'''<br />
{{Structure
|PDB= 1z0h |SIZE=350|CAPTION= <scene name='initialview01'>1z0h</scene>, resolution 2.00&Aring;
|SITE=
|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]
|GENE= botB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1491 Clostridium botulinum])
}}
 
'''N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1Z0H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0H OCA].  
1Z0H is a [[Single protein]] structure of sequence 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=1Z0H OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15781237 15781237]
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:[http://www.ncbi.nlm.nih.gov/pubmed/15781237 15781237]
[[Category: Bontoxilysin]]
[[Category: Bontoxilysin]]
[[Category: Clostridium botulinum]]
[[Category: Clostridium botulinum]]
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[[Category: binding domain]]
[[Category: binding domain]]
[[Category: clostridium botulinum]]
[[Category: clostridium botulinum]]
[[Category: gangliosides]]
[[Category: ganglioside]]
[[Category: x-ray crystallography]]
[[Category: x-ray crystallography]]


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Revision as of 16:29, 20 March 2008

File:1z0h.gif


PDB ID 1z0h

Drag the structure with the mouse to rotate
, resolution 2.00Å
Gene: botB (Clostridium botulinum)
Activity: Bontoxilysin, with EC number 3.4.24.69
Coordinates: save as pdb, mmCIF, xml



N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B


OverviewOverview

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 StructureAbout this Structure

1Z0H is a Single protein structure of sequence from Clostridium botulinum. Full crystallographic information is available from OCA.

ReferenceReference

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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