View source for 9ces


==Guillardia theta Fanzor (GtFz) State 2==
<StructureSection load='9ces' size='340' side='right'caption='[[9ces]], [[Resolution|resolution]] 3.28&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9ces]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12], [https://en.wikipedia.org/wiki/Guillardia_theta Guillardia theta] 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=9CES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9CES 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]] 3.28&#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=9ces FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9ces OCA], [https://pdbe.org/9ces PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9ces RCSB], [https://www.ebi.ac.uk/pdbsum/9ces PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9ces 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/L1JXG4_GUITC L1JXG4_GUITC] 
<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 9ces" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Guillardia theta]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Saito M]]
[[Category: Xu P]]
[[Category: Zhang F]]