6f1s: Difference between revisions
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==C-terminal domain of CglI restriction endonuclease H subunit== | |||
<StructureSection load='6f1s' size='340' side='right'caption='[[6f1s]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6f1s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_glutamicum Corynebacterium glutamicum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F1S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6F1S FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <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=6f1s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f1s OCA], [https://pdbe.org/6f1s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6f1s RCSB], [https://www.ebi.ac.uk/pdbsum/6f1s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6f1s ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/H7C664_CORGT H7C664_CORGT] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
CglI is a restriction endonuclease from Corynebacterium glutamicum that forms a complex between: two R-subunits that have site specific-recognition and nuclease domains; and two H-subunits, with Superfamily 2 helicase-like DEAD domains, and uncharacterized Z1 and C-terminal domains. ATP hydrolysis by the H-subunits catalyses dsDNA translocation that is necessary for long-range movement along DNA that activates nuclease activity. Here, we provide biochemical and molecular modelling evidence that shows that Z1 has a fold distantly-related to RecA, and that the DEAD-Z1 domains together form an ATP binding interface and are the prototype of a previously undescribed monomeric helicase-like motor. The DEAD-Z1 motor has unusual Walker A and Motif VI sequences those nonetheless have their expected functions. Additionally, it contains DEAD-Z1-specific features: an H/H motif and a loop (aa 163-aa 172), that both play a role in the coupling of ATP hydrolysis to DNA cleavage. We also solved the crystal structure of the C-terminal domain which has a unique fold, and demonstrate that the Z1-C domains are the principal DNA binding interface of the H-subunit. Finally, we use small angle X-ray scattering to provide a model for how the H-subunit domains are arranged in a dimeric complex. | |||
The H-subunit of the restriction endonuclease CglI contains a prototype DEAD-Z1 helicase-like motor.,Toliusis P, Tamulaitiene G, Grigaitis R, Tuminauskaite D, Silanskas A, Manakova E, Venclovas C, Szczelkun MD, Siksnys V, Zaremba M Nucleic Acids Res. 2018 Feb 20. pii: 4877023. doi: 10.1093/nar/gky107. PMID:29471489<ref>PMID:29471489</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6f1s" style="background-color:#fffaf0;"></div> | ||
[[Category: Grigaitis | == References == | ||
[[Category: Tamulaitiene | <references/> | ||
[[Category: Zaremba | __TOC__ | ||
</StructureSection> | |||
[[Category: Corynebacterium glutamicum]] | |||
[[Category: Large Structures]] | |||
[[Category: Grigaitis R]] | |||
[[Category: Silanskas A]] | |||
[[Category: Tamulaitiene G]] | |||
[[Category: Zaremba M]] | |||