6F1S

C-terminal domain of CglI restriction endonuclease H subunit

Summary for 6F1S

• Entry DOI: 10.2210/pdb6f1s/pdb
• Descriptor: CglIIR protein, FORMIC ACID, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: restriction endonuclease, ntpase, hydrolase
• Biological source: Corynebacterium glutamicum (Brevibacterium saccharolyticum)
• Total number of polymer chains: 1
• Total formula weight: 20032.29

Authors

Tamulaitiene, G.,Grigaitis, R.,Zaremba, M.,Silanskas, A. (deposition date: 2017-11-23, release date: 2018-02-14, Last modification date: 2024-11-20)

Primary citation

Toliusis, P.,Tamulaitiene, G.,Grigaitis, R.,Tuminauskaite, D.,Silanskas, A.,Manakova, E.,Venclovas, C.,Szczelkun, M.D.,Siksnys, V.,Zaremba, M.
The H-subunit of the restriction endonuclease CglI contains a prototype DEAD-Z1 helicase-like motor.
Nucleic Acids Res., 46:2560-2572, 2018

PubMed Abstract: 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.

PubMed: 29471489
DOI: 10.1093/nar/gky107

Experimental method

X-RAY DIFFRACTION (2.4 Å)