1qii: Difference between revisions

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-{{Seed}}
-[[Image:1qii.png|left|200px]]
-<!--
+==SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE AT NINE TIME POINTS (POINT F) CAUSED BY INTENSE SYNCHROTRON RADIATION TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE==
-The line below this paragraph, containing "STRUCTURE_1qii", creates the "Structure Box" on the page.
+<StructureSection load='1qii' size='340' side='right'caption='[[1qii]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1qii]] 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=1QII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QII FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#8491;</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=1qii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qii OCA], [https://pdbe.org/1qii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qii RCSB], [https://www.ebi.ac.uk/pdbsum/1qii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qii ProSAT]</span></td></tr>
-{{STRUCTURE_1qii|  PDB=1qii  |  SCENE=  }}
+</table>
+== Function ==
+[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 ==
+[[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/qi/1qii_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/main_output.php?pdb_ID=1qii ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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 AT NINE TIME POINTS (POINT F) CAUSED BY INTENSE SYNCHROTRON RADIATION TO TORPEDO CALIFORNICA ACETYLCHOLINESTERASE===
+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<ref>PMID:10639129</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1qii" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_10639129}}, adds the Publication Abstract to the page
+*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 10639129 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_10639129}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-QII is a 1 chain structure of 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=1QII OCA].
+[[Category: Tetronarce californica]]
+[[Category: Kryger G]]
-==Reference==
+[[Category: Ravelli RBG]]
-<ref group="xtra">PMID:10639129</ref><references group="xtra"/>
+[[Category: Weik M]]
-[[Category: Acetylcholinesterase]]
-[[Category: Torpedo californica]]
-[[Category: Kryger, G.]]
-[[Category: Ravelli, R B.G.]]
-[[Category: Weik, M.]]
-[[Category: Alpha/beta hydrolase]]
-[[Category: Catalytic triad]]
-[[Category: Disulfide bond]]
-[[Category: Glycosylated protein]]
-[[Category: Neurotransmitter cleavage]]
-[[Category: Radiation damage]]
-[[Category: Serine hydrolase]]
-[[Category: Time series]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 21:08:00 2009''