Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2019 Jul 11;75(1):90–101.e5. doi: 10.1016/j.molcel.2019.04.020

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2019 The Author(s)

This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

PMC Copyright notice

Conformational Analysis of the Cas1-Cas2 Proteins

(A) The structure of the EfCas1-Cas2 integration complex (Xiao et al., 2017; PDB: 5XVP).

(B) The Cas1-Cas2-Csn2 monomer model with Csn2 (gray) highlighting the positions of Cas1 and Cas2 relative to the bound DNA. The box denotes a single Cas1₄-Cas2₂ complex equivalent to the EfCas1-Cas2 structure in (A). The density corresponding to Cas2 sits between a pair of Cas1 dimers in a similar fashion to the EfCas1-Cas2 structures. However, the bound DNA is separate from Cas2 and rotated by 90° compared to the EfCas1-Cas2 integration structure.

(C) View from the side of the monomer complex with the Cas2 density shown as a transparent surface (green). Cas2 covers a pore between Csn2 tail domains of the adjacent tetramers, thereby blocking access to the bound DNA.