View source for 3zth


==Crystal structure of Stu0660 of Streptococcus thermophilus==
<StructureSection load='3zth' size='340' side='right'caption='[[3zth]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zth]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Strt2 Strt2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZTH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZTH FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=3zth FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zth OCA], [https://pdbe.org/3zth PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zth RCSB], [https://www.ebi.ac.uk/pdbsum/3zth PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zth ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Many prokaryotic organisms acquire immunity against foreign genetic material by incorporating a short segment of foreign DNA called spacer into chromosomal loci, termed clustered regularly interspaced short palindromic repeats (CRISPRs). The encoded RNAs are processed into small fragments that guide the silencing of the invading genetic elements. The CRISPR-associated (Cas) proteins are the main executioners of these processes. Herein, we report the crystal structure of Stu0660 of Streptococcus thermophilus, a Cas protein involved in the acquisition of new spacers. By homotetramerization, Stu0660 forms a central channel which is decorated with basic amino acids and binds linear double-stranded DNA (dsDNA), but not circular dsDNA. Despite undetectably low sequence similarity, two N-terminal domains of Stu0660 are similar to the entire structure of an Enterococcus faecalis Csn2 protein, which also forms a homotetramer and binds dsDNA. Thus, this work identifies a previously unknown group of Stu0660-like Csn2 proteins ( approximately 350 residues), which are larger than the known canonical Csn2 proteins ( approximately 220 residues) by containing an extra C-terminal domain. The commonly present central channel in the two subgroups appears as a design to selectively interact with linear dsDNA. Proteins 2012;. (c) 2012 Wiley Periodicals, Inc.

Identification, structural, and biochemical characterization of a group of large Csn2 proteins involved in CRISPR-mediated bacterial immunity.,Lee KH, Lee SG, Eun Lee K, Jeon H, Robinson H, Oh BH Proteins. 2012 Jul 2. doi: 10.1002/prot.24138. PMID:22753072<ref>PMID:22753072</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zth" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Strt2]]
[[Category: Lee, K H]]
[[Category: Oh, B H]]
[[Category: Robinson, H]]
[[Category: Ca]]
[[Category: Crispr]]
[[Category: Dna binding]]