View source for 9cew


==Spizellomyces punctatus Fanzor (SpuFz) State 3==
<StructureSection load='9cew' size='340' side='right'caption='[[9cew]], [[Resolution|resolution]] 2.88&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9cew]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12], [https://en.wikipedia.org/wiki/Spizellomyces_punctatus Spizellomyces punctatus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9CEW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9CEW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.88&#8491;</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=9cew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9cew OCA], [https://pdbe.org/9cew PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9cew RCSB], [https://www.ebi.ac.uk/pdbsum/9cew PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9cew ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.[https://www.uniprot.org/uniprot/A0A0L0H5U9_SPIPD A0A0L0H5U9_SPIPD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Fanzor (Fz) is an omegaRNA-guided endonuclease extensively found throughout the eukaryotic domain with unique gene editing potential. Here, we describe the structures of Fzs from three different organisms. We find that Fzs share a common omegaRNA interaction interface, regardless of the length of the omegaRNA, which varies considerably across species. The analysis also reveals Fz's mode of DNA recognition and unwinding capabilities as well as the presence of a non-canonical catalytic site. The structures demonstrate how protein conformations of Fz shift to allow the binding of double-stranded DNA to the active site within the R-loop. Mechanistically, examination of structures in different states shows that the conformation of the lid loop on the RuvC domain is controlled by the formation of the guide/DNA heteroduplex, regulating the activation of nuclease and DNA double-stranded displacement at the single cleavage site. Our findings clarify the mechanism of Fz, establishing a foundation for engineering efforts.

Structural insights into the diversity and DNA cleavage mechanism of Fanzor.,Xu P, Saito M, Faure G, Maguire S, Chau-Duy-Tam Vo S, Wilkinson ME, Kuang H, Wang B, Rice WJ, Macrae RK, Zhang F Cell. 2024 Aug 21:S0092-8674(24)00844-4. doi: 10.1016/j.cell.2024.07.050. PMID:39208796<ref>PMID:39208796</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9cew" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Spizellomyces punctatus]]
[[Category: Synthetic construct]]
[[Category: Saito M]]
[[Category: Xu P]]
[[Category: Zhang F]]