3n78

<StructureSection load='3n78' size='340' side='right' caption='[[3n78]], [[Resolution|resolution]] 2.95&Aring;' scene=''>

<table><tr><td colspan='2'>[[3n78]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_griseus Streptomyces griseus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N78 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3N78 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3n7b|3n7b]], [[3dw9|3dw9]], [[3dvo|3dvo]], [[3dgp|3dgp]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SGRA1R, sgraIR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1911 Streptomyces griseus])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3n78 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n78 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3n78 RCSB], [http://www.ebi.ac.uk/pdbsum/3n78 PDBsum]</span></td></tr>

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== Publication Abstract from PubMed ==

SgrAI is a type II restriction endonuclease that cuts an unusually long recognition sequence and exhibits allosteric self-activation with expansion of DNA-sequence specificity. The three-dimensional crystal structures of SgrAI bound to cleaved primary-site DNA and Mg(2)(+) and bound to secondary-site DNA with either Mg(2)(+) or Ca(2)(+) are presented. All three structures show a conformation of enzyme and DNA similar to the previously determined dimeric structure of SgrAI bound to uncleaved primary-site DNA and Ca(2)(+) [Dunten et al. (2008), Nucleic Acids Res. 36, 5405-5416], with the exception of the cleaved bond and a slight shifting of the DNA in the SgrAI/cleaved primary-site DNA/Mg(2)(+) structure. In addition, a new metal ion binding site is located in one of the two active sites in this structure, which is consistent with proposals for the existence of a metal-ion site near the 3'-O leaving group.

 

New clues in the allosteric activation of DNA cleavage by SgrAI: structures of SgrAI bound to cleaved primary-site DNA and uncleaved secondary-site DNA.,Little EJ, Dunten PW, Bitinaite J, Horton NC Acta Crystallogr D Biol Crystallogr. 2011 Jan;67(Pt 1):67-74. Epub 2010, Dec 16. PMID:21206063<ref>PMID:21206063</ref>

 

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<references/>

[[Category: Dunten, P W]]

[[Category: Horton, N C]]

[[Category: Little, E J]]

[[Category: Restriction endonuclease]]