1z7h

From Proteopedia

(Difference between revisions)

Revision as of 16:57, 20 October 2021

2.3 Angstrom crystal structure of tetanus neurotoxin light chain

Structural highlights

1z7h 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:
Gene:	tetX ("Bacillus tetani" Flugge 1886)
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

TeNT is the causative agent of the neuroparalytic disease tetanus. A key component of TeNT is its light chain, a Zn(2+) endopeptidase that targets SNAREs. Recent structural studies of closely related BoNT endopeptidases indicate that substrate-binding exosites remote from a conserved active site are the primary determinants of substrate specificity. Here we report the 2.3 A X-ray crystal structure of TeNT-LC, determined by combined molecular replacement and MAD phasing. As expected, the overall structure of TeNT-LC is similar to the other known CNT light chain structures, including a conserved thermolysin-like core inserted between structurally distinct amino- and carboxy-terminal regions. Differences between TeNT-LC and the other CNT light chains are mainly limited to surface features such as unique electrostatic potential profiles. An analysis of surface residue conservation reveals a pattern of relatively high variability matching the path of substrate binding around BoNT/A, possibly serving to accommodate the variations in different SNARE targets of the CNT group.

2.3 A crystal structure of tetanus neurotoxin light chain.,Breidenbach MA, Brunger AT Biochemistry. 2005 May 24;44(20):7450-7. PMID:15895988^[1]

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

References

↑ Breidenbach MA, Brunger AT. 2.3 A crystal structure of tetanus neurotoxin light chain. Biochemistry. 2005 May 24;44(20):7450-7. PMID:15895988 doi:10.1021/bi050262j

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/1z7h"

@@ Line 3: / Line 3: @@
 <StructureSection load='1z7h' size='340' side='right'caption='[[1z7h]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1z7h]] 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=1Z7H OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Z7H FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1z7h]] 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=1Z7H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z7H FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tetX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1513 "Bacillus tetani" Flugge 1886])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tetX ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1513 "Bacillus tetani" Flugge 1886])</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='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'>[http://proteopedia.org/fgij/fg.htm?mol=1z7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z7h OCA], [http://pdbe.org/1z7h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z7h RCSB], [http://www.ebi.ac.uk/pdbsum/1z7h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z7h 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=1z7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z7h OCA], [https://pdbe.org/1z7h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z7h RCSB], [https://www.ebi.ac.uk/pdbsum/1z7h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z7h 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]]

1z7h

From Proteopedia

Revision as of 16:57, 20 October 2021

2.3 Angstrom crystal structure of tetanus neurotoxin light chain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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