1dfq
From Proteopedia
(Difference between revisions)
| (One intermediate revision not shown.) | |||
| Line 3: | Line 3: | ||
<StructureSection load='1dfq' size='340' side='right'caption='[[1dfq]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='1dfq' size='340' side='right'caption='[[1dfq]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1dfq]] is a 1 chain structure with sequence from [ | + | <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=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id=' | + | <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='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'>[ | + | |
</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. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 21: | Line 20: | ||
</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®/PubMed®, 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: | + | [[Category: Clostridium tetani]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Black I]] | |
| - | [[Category: Black | + | [[Category: Charles IG]] |
| - | [[Category: Charles | + | [[Category: Emsley P]] |
| - | [[Category: Emsley | + | [[Category: Fairweather NF]] |
| - | [[Category: Fairweather | + | [[Category: Fotinou C]] |
| - | [[Category: Fotinou | + | [[Category: Hewitt E]] |
| - | [[Category: Hewitt | + | [[Category: Isaacs NW]] |
| - | [[Category: Isaacs | + | [[Category: Watts C]] |
| - | [[Category: Watts | + | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
THE HC FRAGMENT OF TETANUS TOXIN COMPLEXED WITH SIALIC ACID
| |||||||||||
Categories: Clostridium tetani | Large Structures | Black I | Charles IG | Emsley P | Fairweather NF | Fotinou C | Hewitt E | Isaacs NW | Watts C
