View source for 2lvs


==NMR solution structure of a CRISPR repeat binding protein==
<StructureSection load='2lvs' size='340' side='right'caption='[[2lvs]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lvs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hyperthermus_butylicus_DSM_5456 Hyperthermus butylicus DSM 5456]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LVS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LVS FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lvs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lvs OCA], [https://pdbe.org/2lvs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lvs RCSB], [https://www.ebi.ac.uk/pdbsum/2lvs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lvs ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A2BLH2_HYPBU A2BLH2_HYPBU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Clustered regularly interspaced short palindromic repeats (CRISPR) form the basis of diverse adaptive immune systems directed primarily against invading genetic elements of archaea and bacteria. Cbp1 of the crenarchaeal thermoacidophilic order Sulfolobales, carrying three imperfect repeats, binds specifically to CRISPR DNA repeats and has been implicated in facilitating production of long transcripts from CRISPR loci. Here, a second related class of CRISPR DNA repeat-binding protein, denoted Cbp2, is characterized that contains two imperfect repeats and is found amongst members of the crenarchaeal thermoneutrophilic order Desulfurococcales. DNA repeat-binding properties of the Hyperthermus butylicus protein Cbp2Hb were characterized and its three-dimensional structure was determined by NMR spectroscopy. The two repeats generate helix-turn-helix structures separated by a basic linker that is implicated in facilitating high affinity DNA binding of Cbp2 by tethering the two domains. Structural studies on mutant proteins provide support for Cys(7) and Cys(28) enhancing high thermal stability of Cbp2Hb through disulphide bridge formation. Consistent with their proposed CRISPR transcriptional regulatory role, Cbp2Hb and, by inference, other Cbp1 and Cbp2 proteins are closely related in structure to homeodomain proteins with linked helix-turn-helix (HTH) domains, in particular the paired domain Pax and Myb family proteins that are involved in eukaryal transcriptional regulation.

Solution properties of the archaeal CRISPR DNA repeat-binding homeodomain protein Cbp2.,Kenchappa CS, Heidarsson PO, Kragelund BB, Garrett RA, Poulsen FM Nucleic Acids Res. 2013 Mar 1;41(5):3424-35. doi: 10.1093/nar/gks1465. Epub 2013 , Jan 15. PMID:23325851<ref>PMID:23325851</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lvs" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hyperthermus butylicus DSM 5456]]
[[Category: Large Structures]]
[[Category: Garrett RA]]
[[Category: Heidarsson PO]]
[[Category: Kenchappa CS]]
[[Category: Poulsen FM]]