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New page: left|200px<br /><applet load="1zb7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zb7, resolution 2.35Å" /> '''Crystal Structure of...
 
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[[Image:1zb7.gif|left|200px]]<br /><applet load="1zb7" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1zb7, resolution 2.35&Aring;" />
'''Crystal Structure of Botulinum Neurotoxin Type G Light Chain'''<br />


==Overview==
==Crystal Structure of Botulinum Neurotoxin Type G Light Chain==
The seven serotypes (A-G) of botulinum neurotoxins (BoNTs) block, neurotransmitter release through their specific proteolysis of one of the, three proteins of the soluble N-ethylmaleimide-sensitive-factor attachment, protein receptor (SNARE) complex. BoNTs have stringent substrate, specificities that are unique for metalloprotease in that they require, exceptionally long substrates (1). To understand the molecular reasons for, the unique specificities of the BoNTs, we determined the crystal structure, of the catalytic light chain (LC) of Clostridium botulinum neurotoxin type, G (BoNT/G-LC) at 2.35 A resolution. The structure of BoNT/G-LC reveals a, C-terminal beta-sheet that is critical for LC oligomerization and is, unlike that seen in the other LC structures. Its structural comparison, with thermolysin and the available pool of LC structures reveals important, serotype differences that are likely to be involved in substrate, recognition of the P1' residue. In addition, structural and sequence, analyses have identified a potential exosite of BoNT/G-LC that recognizes, a SNARE recognition motif of VAMP.
<StructureSection load='1zb7' size='340' side='right'caption='[[1zb7]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1zb7]] is a 1 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=1ZB7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZB7 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]] 2.35&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</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=1zb7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zb7 OCA], [https://pdbe.org/1zb7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zb7 RCSB], [https://www.ebi.ac.uk/pdbsum/1zb7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zb7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BXG_CLOBO BXG_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.
== 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/zb/1zb7_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1zb7 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The seven serotypes (A-G) of botulinum neurotoxins (BoNTs) block neurotransmitter release through their specific proteolysis of one of the three proteins of the soluble N-ethylmaleimide-sensitive-factor attachment protein receptor (SNARE) complex. BoNTs have stringent substrate specificities that are unique for metalloprotease in that they require exceptionally long substrates (1). To understand the molecular reasons for the unique specificities of the BoNTs, we determined the crystal structure of the catalytic light chain (LC) of Clostridium botulinum neurotoxin type G (BoNT/G-LC) at 2.35 A resolution. The structure of BoNT/G-LC reveals a C-terminal beta-sheet that is critical for LC oligomerization and is unlike that seen in the other LC structures. Its structural comparison with thermolysin and the available pool of LC structures reveals important serotype differences that are likely to be involved in substrate recognition of the P1' residue. In addition, structural and sequence analyses have identified a potential exosite of BoNT/G-LC that recognizes a SNARE recognition motif of VAMP.


==About this Structure==
Crystal structure of botulinum neurotoxin type G light chain: serotype divergence in substrate recognition.,Arndt JW, Yu W, Bi F, Stevens RC Biochemistry. 2005 Jul 19;44(28):9574-80. PMID:16008342<ref>PMID:16008342</ref>
1ZB7 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 FLC as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZB7 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of botulinum neurotoxin type G light chain: serotype divergence in substrate recognition., Arndt JW, Yu W, Bi F, Stevens RC, Biochemistry. 2005 Jul 19;44(28):9574-80. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16008342 16008342]
</div>
<div class="pdbe-citations 1zb7" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Botulinum neurotoxin 3D structures|Botulinum neurotoxin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clostridium botulinum]]
[[Category: Clostridium botulinum]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Arndt, J.W.]]
[[Category: Arndt JW]]
[[Category: Bi, F.]]
[[Category: Bi F]]
[[Category: Stevens, R.C.]]
[[Category: Stevens RC]]
[[Category: Yu, W.]]
[[Category: Yu W]]
[[Category: FLC]]
[[Category: ZN]]
[[Category: hexxh metalloprotease]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:21:33 2007''

Latest revision as of 07:44, 30 October 2024

Crystal Structure of Botulinum Neurotoxin Type G Light Chain

1zb7, resolution 2.35Å

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