4p6i
From Proteopedia
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<StructureSection load='4p6i' size='340' side='right' caption='[[4p6i]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='4p6i' size='340' side='right' caption='[[4p6i]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4p6i]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P6I OCA]. | + | <table><tr><td colspan='2'>[[4p6i]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P6I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P6I FirstGlance]. <br> |
| - | + | </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=4p6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p6i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p6i RCSB], [http://www.ebi.ac.uk/pdbsum/4p6i PDBsum]</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=4p6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p6i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p6i RCSB], [http://www.ebi.ac.uk/pdbsum/4p6i PDBsum]</span></td></tr> | + | |
<table> | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The initial stage of CRISPR-Cas immunity involves the integration of foreign DNA spacer segments into the host genomic CRISPR locus. The nucleases Cas1 and Cas2 are the only proteins conserved among all CRISPR-Cas systems, yet the molecular functions of these proteins during immunity are unknown. Here we show that Cas1 and Cas2 from Escherichia coli form a stable complex that is essential for spacer acquisition and determine the 2.3-A-resolution crystal structure of the Cas1-Cas2 complex. Mutations that perturb Cas1-Cas2 complex formation disrupt CRISPR DNA recognition and spacer acquisition in vivo. Active site mutants of Cas2, unlike those of Cas1, can still acquire new spacers, thus indicating a nonenzymatic role of Cas2 during immunity. These results reveal the universal roles of Cas1 and Cas2 and suggest a mechanism by which Cas1-Cas2 complexes specify sites of CRISPR spacer integration. | ||
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| + | Cas1-Cas2 complex formation mediates spacer acquisition during CRISPR-Cas adaptive immunity.,Nunez JK, Kranzusch PJ, Noeske J, Wright AV, Davies CW, Doudna JA Nat Struct Mol Biol. 2014 May 4. doi: 10.1038/nsmb.2820. PMID:24793649<ref>PMID:24793649</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 07:00, 21 May 2014
Crystal structure of the Cas1-Cas2 complex from Escherichia coli
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