View source for 8aa5


==Cryo-EM structure of the strand transfer complex of the TnsB transposase (type V-K CRISPR-associated transposon)==
<StructureSection load='8aa5' size='340' side='right'caption='[[8aa5]], [[Resolution|resolution]] 2.46&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8aa5]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Scytonema_hofmannii Scytonema hofmannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8AA5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8AA5 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]] 2.46&#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=8aa5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8aa5 OCA], [https://pdbe.org/8aa5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8aa5 RCSB], [https://www.ebi.ac.uk/pdbsum/8aa5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8aa5 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
CRISPR-associated transposons (CASTs) are mobile genetic elements that co-opted CRISPR-Cas systems for RNA-guided transposition. Here we present the 2.4 A cryo-EM structure of the Scytonema hofmannii (sh) TnsB transposase from Type V-K CAST, bound to the strand transfer DNA. The strand transfer complex displays an intertwined pseudo-symmetrical architecture. Two protomers involved in strand transfer display a catalytically competent active site composed by DDE residues, while other two, which play a key structural role, show active sites where the catalytic residues are not properly positioned for phosphodiester hydrolysis. Transposon end recognition is accomplished by the NTD1/2 helical domains. A singular in trans association of NTD1 domains of the catalytically competent subunits with the inactive DDE domains reinforces the assembly. Collectively, the structural features suggest that catalysis is coupled to protein-DNA assembly to secure proper DNA integration. DNA binding residue mutants reveal that lack of specificity decreases activity, but it could increase transposition in some cases. Our structure sheds light on the strand transfer reaction of DDE transposases and offers new insights into CAST transposition.

Structure of the TnsB transposase-DNA complex of type V-K CRISPR-associated transposon.,Tenjo-Castano F, Sofos N, Lopez-Mendez B, Stutzke LS, Fuglsang A, Stella S, Montoya G Nat Commun. 2022 Oct 2;13(1):5792. doi: 10.1038/s41467-022-33504-5. PMID:36184667<ref>PMID:36184667</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Transposase 3D structures|Transposase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Scytonema hofmannii]]
[[Category: Fuglsang A]]
[[Category: Lopez-Mendez B]]
[[Category: Montoya G]]
[[Category: Sofos N]]
[[Category: Stella S]]
[[Category: Stutzke LS]]
[[Category: Tenjo-Castano F]]