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[[Image: | ==TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH A NON HYDROLYSABLE SUBSTRATE ANALOGUE, 4-OXO-N,N,N-TRIMETHYLPENTANAMINIUM - ORTHORHOMBIC SPACE GROUP -DATASET C AT 150K== | ||
<StructureSection load='2vjd' size='340' side='right' caption='[[2vjd]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2vjd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Torpedo_californica Torpedo californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VJD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VJD FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CCD:(4R)-4-HYDROXY-N,N,N-TRIMETHYLPENTAN-1-AMINIUM'>CCD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zgb|1zgb]], [[1qti|1qti]], [[1amn|1amn]], [[1e66|1e66]], [[2vq6|2vq6]], [[2j3d|2j3d]], [[2ack|2ack]], [[1qii|1qii]], [[2ckm|2ckm]], [[1dx6|1dx6]], [[1qij|1qij]], [[1qie|1qie]], [[1acl|1acl]], [[1w4l|1w4l]], [[1odc|1odc]], [[2cmf|2cmf]], [[2j3q|2j3q]], [[1gqs|1gqs]], [[2j4f|2j4f]], [[1e3q|1e3q]], [[2dfp|2dfp]], [[1qik|1qik]], [[2c5f|2c5f]], [[1ea5|1ea5]], [[2vjc|2vjc]], [[1eea|1eea]], [[1qif|1qif]], [[2vjb|2vjb]], [[1qig|1qig]], [[1zgc|1zgc]], [[1qid|1qid]], [[1jjb|1jjb]], [[1ut6|1ut6]], [[2vt6|2vt6]], [[2vt7|2vt7]], [[2cek|2cek]], [[1qim|1qim]], [[1gpk|1gpk]], [[1jga|1jga]], [[3ace|3ace]], [[1oce|1oce]], [[1w6r|1w6r]], [[1som|1som]], [[1vxo|1vxo]], [[2vja|2vja]], [[1cfj|1cfj]], [[2v96|2v96]], [[1ax9|1ax9]], [[1u65|1u65]], [[1w76|1w76]], [[1h22|1h22]], [[1eve|1eve]], [[2c4h|2c4h]], [[1gqr|1gqr]], [[2ace|2ace]], [[2va9|2va9]], [[1vxr|1vxr]], [[4ace|4ace]], [[2c58|2c58]], [[1hbj|1hbj]], [[1vot|1vot]], [[1w75|1w75]], [[2c5g|2c5g]], [[1jgb|1jgb]], [[2v98|2v98]], [[1gpn|1gpn]], [[1qih|1qih]], [[1h23|1h23]], [[1acj|1acj]], [[1fss|1fss]], [[2v97|2v97]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetylcholinesterase Acetylcholinesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.7 3.1.1.7] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vjd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vjd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vjd RCSB], [http://www.ebi.ac.uk/pdbsum/2vjd PDBsum]</span></td></tr> | |||
<table> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vj/2vjd_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Although x-ray crystallography is the most widely used method for macromolecular structure determination, it does not provide dynamical information, and either experimental tricks or complementary experiments must be used to overcome the inherently static nature of crystallographic structures. Here we used specific x-ray damage during temperature-controlled crystallographic experiments at a third-generation synchrotron source to trigger and monitor (Shoot-and-Trap) structural changes putatively involved in an enzymatic reaction. In particular, a nonhydrolyzable substrate analogue of acetylcholinesterase, the "off-switch" at cholinergic synapses, was radiocleaved within the buried enzymatic active site. Subsequent product clearance, observed at 150 K but not at 100 K, indicated exit from the active site possibly via a "backdoor." The simple strategy described here is, in principle, applicable to any enzyme whose structure in complex with a substrate analogue is available and, therefore, could serve as a standard procedure in kinetic crystallography studies. | |||
Shoot-and-Trap: use of specific x-ray damage to study structural protein dynamics by temperature-controlled cryo-crystallography.,Colletier JP, Bourgeois D, Sanson B, Fournier D, Sussman JL, Silman I, Weik M Proc Natl Acad Sci U S A. 2008 Aug 19;105(33):11742-7. Epub 2008 Aug 13. PMID:18701720<ref>PMID:18701720</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Acetylcholinesterase|Acetylcholinesterase]] | *[[Acetylcholinesterase|Acetylcholinesterase]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Acetylcholinesterase]] | [[Category: Acetylcholinesterase]] | ||
[[Category: Torpedo californica]] | [[Category: Torpedo californica]] | ||
Revision as of 12:04, 29 September 2014
TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH A NON HYDROLYSABLE SUBSTRATE ANALOGUE, 4-OXO-N,N,N-TRIMETHYLPENTANAMINIUM - ORTHORHOMBIC SPACE GROUP -DATASET C AT 150KTORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH A NON HYDROLYSABLE SUBSTRATE ANALOGUE, 4-OXO-N,N,N-TRIMETHYLPENTANAMINIUM - ORTHORHOMBIC SPACE GROUP -DATASET C AT 150K
Structural highlights
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 PubMedAlthough x-ray crystallography is the most widely used method for macromolecular structure determination, it does not provide dynamical information, and either experimental tricks or complementary experiments must be used to overcome the inherently static nature of crystallographic structures. Here we used specific x-ray damage during temperature-controlled crystallographic experiments at a third-generation synchrotron source to trigger and monitor (Shoot-and-Trap) structural changes putatively involved in an enzymatic reaction. In particular, a nonhydrolyzable substrate analogue of acetylcholinesterase, the "off-switch" at cholinergic synapses, was radiocleaved within the buried enzymatic active site. Subsequent product clearance, observed at 150 K but not at 100 K, indicated exit from the active site possibly via a "backdoor." The simple strategy described here is, in principle, applicable to any enzyme whose structure in complex with a substrate analogue is available and, therefore, could serve as a standard procedure in kinetic crystallography studies. Shoot-and-Trap: use of specific x-ray damage to study structural protein dynamics by temperature-controlled cryo-crystallography.,Colletier JP, Bourgeois D, Sanson B, Fournier D, Sussman JL, Silman I, Weik M Proc Natl Acad Sci U S A. 2008 Aug 19;105(33):11742-7. Epub 2008 Aug 13. PMID:18701720[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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