1yyn

From Proteopedia

(Difference between revisions)

Revision as of 16:34, 3 November 2021

A common binding site for disialyllactose and a tri-peptide in the C-fragment of tetanus neurotoxin

Structural highlights

1yyn is a 1 chain structure with sequence from "bacillus_tetani"_flugge_1886 "bacillus tetani" flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Related:	1af9
Activity:	Tentoxilysin, with EC number 3.4.24.68
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.

Publication Abstract from PubMed

Clostridial neurotoxins are comprised of botulinum (BoNT) and tetanus (TeNT), which share significant structural and functional similarity. Crystal structures of the binding domain of TeNT complexed with disialyllactose (DiSia) and a tri-peptide Tyr-Glu-Trp (YEW) have been determined to 2.3 and 2.2 A, respectively. Both DiSia and YEW bind in a shallow cleft region on the surface of the molecule in the beta-trefoil domain, interacting with a set of common residues, Asp1147, Asp1214, Asn1216, and Arg1226. DiSia and YEW binding at the same site in tetanus toxin provides a putative site that could be occupied either by a ganglioside moiety or a peptide. Soaking experiments with a mixture of YEW and DiSia show that YEW competes with DiSia, suggesting that YEW can be used to block ganglioside binding. A comparison with the TeNT binding domain in complex with small molecules, BoNT/A and /B, provides insight into the different modes of ganglioside binding.

Common binding site for disialyllactose and tri-peptide in C-fragment of tetanus neurotoxin.,Jayaraman S, Eswaramoorthy S, Kumaran D, Swaminathan S Proteins. 2005 Nov 1;61(2):288-95. PMID:16104015^[1]

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

References

↑ Jayaraman S, Eswaramoorthy S, Kumaran D, Swaminathan S. Common binding site for disialyllactose and tri-peptide in C-fragment of tetanus neurotoxin. Proteins. 2005 Nov 1;61(2):288-95. PMID:16104015 doi:10.1002/prot.20595

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/1yyn"

@@ Line 3: / Line 3: @@
 <StructureSection load='1yyn' size='340' side='right'caption='[[1yyn]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1yyn]] is a 1 chain structure with sequence from [http://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=1YYN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YYN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1yyn]] 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=1YYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YYN FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1af9|1af9]]</td></tr>
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SIA:O-SIALIC+ACID'>SIA</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tentoxilysin Tentoxilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.68 3.4.24.68] </span></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1af9|1af9]]</div></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=1yyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yyn OCA], [http://pdbe.org/1yyn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yyn RCSB], [http://www.ebi.ac.uk/pdbsum/1yyn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yyn ProSAT]</span></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=1yyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yyn OCA], [https://pdbe.org/1yyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yyn RCSB], [https://www.ebi.ac.uk/pdbsum/1yyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yyn ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

1yyn

From Proteopedia

Revision as of 16:34, 3 November 2021

A common binding site for disialyllactose and a tri-peptide in the C-fragment of tetanus neurotoxin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox