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| | <StructureSection load='1qih' size='340' side='right'caption='[[1qih]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='1qih' size='340' side='right'caption='[[1qih]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1qih]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QIH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1qih]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetronarce_californica Tetronarce californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QIH FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qid|1qid]], [[1qie|1qie]], [[1qif|1qif]], [[1qig|1qig]], [[1qii|1qii]], [[1qij|1qij]], [[1qik|1qik]], [[1qim|1qim]]</div></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]] 2.5Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7] </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=1qih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qih OCA], [https://pdbe.org/1qih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qih RCSB], [https://www.ebi.ac.uk/pdbsum/1qih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qih 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=1qih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qih OCA], [https://pdbe.org/1qih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qih RCSB], [https://www.ebi.ac.uk/pdbsum/1qih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qih ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/ACES_TORCA ACES_TORCA]] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions.
| + | [https://www.uniprot.org/uniprot/ACES_TETCF ACES_TETCF] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Acetylcholinesterase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Torpedo californica]] | + | [[Category: Tetronarce californica]] |
| - | [[Category: Kryger, G]] | + | [[Category: Kryger G]] |
| - | [[Category: Ravelli, R B.G]] | + | [[Category: Ravelli RBG]] |
| - | [[Category: Weik, M]] | + | [[Category: Weik M]] |
| - | [[Category: Alpha/beta hydrolase]]
| + | |
| - | [[Category: Catalytic triad]]
| + | |
| - | [[Category: Disulfide bond]]
| + | |
| - | [[Category: Glycosylated protein]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Neurotransmitter cleavage]]
| + | |
| - | [[Category: Radiation damage]]
| + | |
| - | [[Category: Serine hydrolase]]
| + | |
| - | [[Category: Time series]]
| + | |
| Structural highlights
Function
ACES_TETCF Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions.
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
Radiation damage is an inherent problem in x-ray crystallography. It usually is presumed to be nonspecific and manifested as a gradual decay in the overall quality of data obtained for a given crystal as data collection proceeds. Based on third-generation synchrotron x-ray data, collected at cryogenic temperatures, we show for the enzymes Torpedo californica acetylcholinesterase and hen egg white lysozyme that synchrotron radiation also can cause highly specific damage. Disulfide bridges break, and carboxyl groups of acidic residues lose their definition. Highly exposed carboxyls, and those in the active site of both enzymes, appear particularly susceptible. The catalytic triad residue, His-440, in acetylcholinesterase, also appears to be much more sensitive to radiation damage than other histidine residues. Our findings have direct practical implications for routine x-ray data collection at high-energy synchrotron sources. Furthermore, they provide a direct approach for studying the radiation chemistry of proteins and nucleic acids at a detailed, structural level and also may yield information concerning putative "weak links" in a given biological macromolecule, which may be of structural and functional significance.
Specific chemical and structural damage to proteins produced by synchrotron radiation.,Weik M, Ravelli RB, Kryger G, McSweeney S, Raves ML, Harel M, Gros P, Silman I, Kroon J, Sussman JL Proc Natl Acad Sci U S A. 2000 Jan 18;97(2):623-8. PMID:10639129[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Weik M, Ravelli RB, Kryger G, McSweeney S, Raves ML, Harel M, Gros P, Silman I, Kroon J, Sussman JL. Specific chemical and structural damage to proteins produced by synchrotron radiation. Proc Natl Acad Sci U S A. 2000 Jan 18;97(2):623-8. PMID:10639129
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