1z0h

From Proteopedia

(Difference between revisions)

Revision as of 08:56, 20 January 2021

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

Structural highlights

1z0h is a 2 chain structure with sequence from "bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1erw
Gene:	botB ("Bacillus botulinus" van Ermengem 1896)
Activity:	Bontoxilysin, with EC number 3.4.24.69
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[BXB_CLOBO] Botulinum toxin acts by inhibiting neurotransmitter release. It binds to peripheral neuronal synapses, is internalized and moves by retrograde transport up the axon into the spinal cord where it can move between postsynaptic and presynaptic neurons. It inhibits neurotransmitter release by acting as a zinc endopeptidase that cleaves the '76-Gln-|-Phe-77' bond of synaptobrevin-2.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Jayaraman S, Eswaramoorthy S, Ahmed SA, Smith LA, Swaminathan S. N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B. Biochem Biophys Res Commun. 2005 Apr 29;330(1):97-103. PMID:15781237 doi:http://dx.doi.org/10.1016/j.bbrc.2005.02.123

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1z0h"

@@ Line 1: / Line 1: @@
 ==N-terminal helix reorients in recombinant C-fragment of Clostridium botulinum type B==
-<StructureSection load='1z0h' size='340' side='right' caption='[[1z0h]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='1z0h' size='340' side='right'caption='[[1z0h]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1z0h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z0H FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1z0h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_botulinus"_van_ermengem_1896 "bacillus botulinus" van ermengem 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z0H OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Z0H FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1erw|1erw]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1erw|1erw]]</div></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">botB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1491 "Bacillus botulinus" van Ermengem 1896])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1z0h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z0h RCSB], [http://www.ebi.ac.uk/pdbsum/1z0h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z0h ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1z0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z0h OCA], [http://pdbe.org/1z0h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z0h RCSB], [http://www.ebi.ac.uk/pdbsum/1z0h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z0h ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 32: / Line 32: @@
 ==See Also==
-*[[Botulinum neurotoxin|Botulinum neurotoxin]]
+*[[Botulinum neurotoxin 3D structures|Botulinum neurotoxin 3D structures]]
 == References ==
 <references/>
@@ Line 39: / Line 39: @@
 [[Category: Bacillus botulinus van ermengem 1896]]
 [[Category: Bontoxilysin]]
+[[Category: Large Structures]]
 [[Category: Ashraf, S A]]
 [[Category: Eswarmoorthy, S]]

1z0h

From Proteopedia

Revision as of 08:56, 20 January 2021

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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