Summary information and primary citation
- PDB-id
-
7lo5;
DSSR-derived features in text and
JSON formats
- Class
- hydrolase-DNA
- Method
- cryo-EM (2.86 Å)
- Summary
- Cryoem structure drdv-DNA complex
- Reference
-
Shen BW, Quispe JD, Luyten Y, McGough BE, Morgan RD,
Stoddard BL (2021): "Coordination
of phage genome degradation versus host genome protection
by a bifunctional restriction-modification enzyme
visualized by CryoEM." Structure,
29, 521-530.e5. doi: 10.1016/j.str.2021.03.012.
- Abstract
- Restriction enzymes that combine methylation and
cleavage into a single assemblage and modify one DNA strand
are capable of efficient adaptation toward novel targets.
However, they must reliably cleave invasive DNA and
methylate newly replicated unmodified host sites. One
possible solution is to enforce a competition between slow
methylation at a single unmodified host target, versus
faster cleavage that requires multiple unmodified target
sites in foreign DNA to be brought together in a reaction
synapse. To examine this model, we have determined the
catalytic behavior of a bifunctional type IIL
restriction-modification enzyme and determined its
structure, via cryoelectron microscopy, at several
different stages of assembly and coordination with bound
DNA targets. The structures demonstrate a mechanism in
which an initial dimer is formed between two DNA-bound
enzyme molecules, positioning the endonuclease domain from
each enzyme against the other's DNA and requiring further
additional DNA-bound enzyme molecules to enable
cleavage.
