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[[Image:1t3a.gif|left|200px]]<br />
<applet load="1t3a" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1t3a, resolution 2.16&Aring;" />
'''Crystal structure of Clostridium botulinum neurotoxin type E catalytic domain'''<br />


==Overview==
==Crystal structure of Clostridium botulinum neurotoxin type E catalytic domain==
The seven serotypes of botulinum neurotoxins (A-G) produced by Clostridium, botulinum share significant sequence homology and structural similarity., The functions of their individual domains and the modes of action are also, similar. However, the substrate specificity and the peptide bond cleavage, selectivity of their catalytic domains are different. The reason for this, unique specificity of botulinum neurotoxins is still baffling. If an, inhibitor leading to a therapeutic drug common to all serotypes is to be, developed, it is essential to understand the differences in their, three-dimensional structures that empower them with this unique, characteristic. Accordingly, high-resolution structures of all serotypes, are required, and toward achieving this goal the crystal structure of ... [[http://ispc.weizmann.ac.il/pmbin/getpm?15157097 (full description)]]
<StructureSection load='1t3a' size='340' side='right'caption='[[1t3a]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1t3a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T3A FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.16&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t3a OCA], [https://pdbe.org/1t3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t3a RCSB], [https://www.ebi.ac.uk/pdbsum/1t3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t3a ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BXE_CLOBO BXE_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 catalyzes the hydrolysis of the 180-Arg-|-Ile-181 bond in SNAP-25.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t3/1t3a_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1t3a ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1T3A is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum]] with ZN and CL as [[http://en.wikipedia.org/wiki/ligands ligands]]. 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]]. Structure known Active Sites: AC1 and AC2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T3A OCA]].
*[[Botulinum neurotoxin 3D structures|Botulinum neurotoxin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structural analysis of botulinum neurotoxin type E catalytic domain and its mutant Glu212--&gt;Gln reveals the pivotal role of the Glu212 carboxylate in the catalytic pathway., Agarwal R, Eswaramoorthy S, Kumaran D, Binz T, Swaminathan S, Biochemistry. 2004 Jun 1;43(21):6637-44. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15157097 15157097]
[[Category: Bontoxilysin]]
[[Category: Clostridium botulinum]]
[[Category: Clostridium botulinum]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Agarwal, R.]]
[[Category: Agarwal R]]
[[Category: Binz, T.]]
[[Category: Binz T]]
[[Category: Eswaramoorthy, S.]]
[[Category: Eswaramoorthy S]]
[[Category: Kumaran, D.]]
[[Category: Kumaran D]]
[[Category: Swaminathan, S.]]
[[Category: Swaminathan S]]
[[Category: CL]]
[[Category: ZN]]
[[Category: catalytic domain]]
[[Category: clostridium botulinum]]
[[Category: light chain]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:41:53 2007''

Latest revision as of 11:35, 14 February 2024

Crystal structure of Clostridium botulinum neurotoxin type E catalytic domainCrystal structure of Clostridium botulinum neurotoxin type E catalytic domain

Structural highlights

1t3a is a 2 chain structure with sequence from Clostridium botulinum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.16Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BXE_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 catalyzes the hydrolysis of the 180-Arg-|-Ile-181 bond in SNAP-25.

Evolutionary Conservation

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

See Also

1t3a, resolution 2.16Å

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