4h79
From Proteopedia
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| - | [[Image:4h79.png|left|200px]] | ||
| - | + | ==Crystal structure of CasB from Thermobifida fusca== | |
| + | <StructureSection load='4h79' size='340' side='right' caption='[[4h79]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4h79]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thefy Thefy]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H79 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4H79 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tfu_1599 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=269800 THEFY])</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=4h79 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h79 OCA], [http://pdbe.org/4h79 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4h79 RCSB], [http://www.ebi.ac.uk/pdbsum/4h79 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4h79 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The CRISPR system is an adaptive RNA-based microbial immune system against invasive genetic elements. CasB is an essential protein component in Type I-E Cascade. Here, we characterize CasB proteins from three different organisms as non-specific nucleic acid binding proteins. The Thermobifida fusca CasB crystal structure reveals conserved positive surface charges, which we show are important for its nucleic acid binding function. EM docking reveals that CasB dimerization aligns individual nucleic acid binding surfaces into a curved, elongated binding surface inside Type I-E Cascade, consistent with the putative functions of CasB in ds-DNA recruitment and crRNA-DNA duplex formation steps. STRUCTURED SUMMARY OF PROTEIN INTERACTIONS: TthCasB and TthCasBbind by x-ray crystallography (View interaction) TfuCasB1 and TfuCasB1bind by molecular sieving (View Interaction: 1, 2). | ||
| - | + | Nucleic acid binding surface and dimer interface revealed by CRISPR-associated CasB protein structures.,Nam KH, Huang Q, Ke A FEBS Lett. 2012 Nov 16;586(22):3956-61. doi: 10.1016/j.febslet.2012.09.041. Epub , 2012 Oct 16. PMID:23079036<ref>PMID:23079036</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4h79" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | [[ | + | *[[Endonuclease|Endonuclease]] |
| - | [[Category: | + | == References == |
| - | [[Category: Ke, A | + | <references/> |
| - | [[Category: Nam, K H | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Thefy]] | ||
| + | [[Category: Ke, A]] | ||
| + | [[Category: Nam, K H]] | ||
[[Category: Casb]] | [[Category: Casb]] | ||
[[Category: Cascade]] | [[Category: Cascade]] | ||
Revision as of 19:26, 4 August 2016
Crystal structure of CasB from Thermobifida fusca
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