1dfq: Difference between revisions

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<StructureSection load='1dfq' size='340' side='right'caption='[[1dfq]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='1dfq' size='340' side='right'caption='[[1dfq]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1dfq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_tetani"_flugge_1886 "bacillus tetani" flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DFQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[1dfq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_tetani Clostridium tetani]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DFQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SLB:5-N-ACETYL-BETA-D-NEURAMINIC+ACID'>SLB</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1d0h|1d0h]], [[1af9|1af9]], [[1a8d|1a8d]], [[1diw|1diw]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SLB:5-N-ACETYL-BETA-D-NEURAMINIC+ACID'>SLB</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Tentoxilysin Tentoxilysin], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.68 3.4.24.68] </span></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=1dfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dfq OCA], [https://pdbe.org/1dfq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dfq RCSB], [https://www.ebi.ac.uk/pdbsum/1dfq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dfq ProSAT]</span></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=1dfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dfq OCA], [https://pdbe.org/1dfq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dfq RCSB], [https://www.ebi.ac.uk/pdbsum/1dfq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dfq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/TETX_CLOTE TETX_CLOTE]] Tetanus 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 '76-Gln-|-Phe-77' bond of synaptobrevin-2.  
[https://www.uniprot.org/uniprot/TETX_CLOTE TETX_CLOTE] Tetanus 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 '76-Gln-|-Phe-77' bond of synaptobrevin-2.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1dfq ConSurf].
</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=1dfq ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The entry of tetanus neurotoxin into neuronal cells proceeds through the initial binding of the toxin to gangliosides on the cell surface. The carboxyl-terminal fragment of the heavy chain of tetanus neurotoxin contains the ganglioside-binding site, which has not yet been fully characterized. The crystal structures of native H(C) and of H(C) soaked with carbohydrates reveal a number of binding sites and provide insight into the possible mode of ganglioside binding.
The structures of the H(C) fragment of tetanus toxin with carbohydrate subunit complexes provide insight into ganglioside binding.,Emsley P, Fotinou C, Black I, Fairweather NF, Charles IG, Watts C, Hewitt E, Isaacs NW J Biol Chem. 2000 Mar 24;275(12):8889-94. PMID:10722735<ref>PMID:10722735</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1dfq" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Tetanus toxin|Tetanus toxin]]
*[[Tetanus toxin|Tetanus toxin]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus tetani flugge 1886]]
[[Category: Clostridium tetani]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Tentoxilysin]]
[[Category: Black I]]
[[Category: Black, I]]
[[Category: Charles IG]]
[[Category: Charles, I G]]
[[Category: Emsley P]]
[[Category: Emsley, P]]
[[Category: Fairweather NF]]
[[Category: Fairweather, N F]]
[[Category: Fotinou C]]
[[Category: Fotinou, C]]
[[Category: Hewitt E]]
[[Category: Hewitt, E]]
[[Category: Isaacs NW]]
[[Category: Isaacs, N W]]
[[Category: Watts C]]
[[Category: Watts, C]]
[[Category: Beta trefoil]]
[[Category: Carbohydrate]]
[[Category: Jelly-roll]]
[[Category: Toxin]]

Latest revision as of 09:53, 7 February 2024

THE HC FRAGMENT OF TETANUS TOXIN COMPLEXED WITH SIALIC ACIDTHE HC FRAGMENT OF TETANUS TOXIN COMPLEXED WITH SIALIC ACID

Structural highlights

1dfq is a 1 chain structure with sequence from Clostridium tetani. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TETX_CLOTE Tetanus 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 '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.

See Also

1dfq, resolution 2.60Å

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