1na6: Difference between revisions

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 <StructureSection load='1na6' size='340' side='right'caption='[[1na6]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1na6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NA6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1NA6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1na6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NA6 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EcoRII ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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]] 2.1&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Type_II_site-specific_deoxyribonuclease Type II site-specific deoxyribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.4 3.1.21.4] </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=1na6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1na6 OCA], [https://pdbe.org/1na6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1na6 RCSB], [https://www.ebi.ac.uk/pdbsum/1na6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1na6 ProSAT]</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=1na6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1na6 OCA], [http://pdbe.org/1na6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1na6 RCSB], [http://www.ebi.ac.uk/pdbsum/1na6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1na6 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/T2E2_ECOLX T2E2_ECOLX] Recognizes the double-stranded sequence CCWGG and cleaves before C-1.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </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=1na6 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-EcoRII is a type IIE restriction endonuclease that interacts with two copies of the DNA recognition sequence 5'CCWGG, one being the actual target of cleavage, the other serving as the allosteric effector. The mode of enzyme activation by effector binding is unknown. To investigate the molecular basis of activation and cleavage mechanisms by EcoRII, the crystal structure of EcoRII mutant R88A has been solved at 2.1A resolution. The EcoRII monomer has two domains linked through a hinge loop. The N-terminal effector-binding domain has a novel DNA recognition fold with a prominent cleft. The C-terminal catalytic domain has a restriction endonuclease-like fold. Structure-based sequence alignment identified the putative catalytic site of EcoRII that is spatially blocked by the N-terminal domain. The structure together with the earlier characterized EcoRII enzyme activity enhancement in the absence of its N-terminal domain reveal an autoinhibition/activation mechanism of enzyme activity mediated by a novel effector-binding fold. This is the first case of autoinhibition, a mechanism described for many transcription factors and signal transducing proteins, of a restriction endonuclease.
-Crystal structure of type IIE restriction endonuclease EcoRII reveals an autoinhibition mechanism by a novel effector-binding fold.,Zhou XE, Wang Y, Reuter M, Mucke M, Kruger DH, Meehan EJ, Chen L J Mol Biol. 2004 Jan 2;335(1):307-19. PMID:14659759<ref>PMID:14659759</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1na6" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Endonuclease 3D structures|Endonuclease 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Type II site-specific deoxyribonuclease]]
+[[Category: Chen L]]
-[[Category: Chen, L]]
+[[Category: Kruger DH]]
-[[Category: Kruger, D H]]
+[[Category: Meehan EJ]]
-[[Category: Meehan, E J]]
+[[Category: Mucke M]]
-[[Category: Mucke, M]]
+[[Category: Reuter M]]
-[[Category: Reuter, M]]
+[[Category: Wang Y]]
-[[Category: Wang, Y]]
+[[Category: Zhou XE]]
-[[Category: Zhou, X E]]
-[[Category: Hydrolase]]
-[[Category: Mutation]]
-[[Category: Replication]]
-[[Category: Site-specific restriction]]