Structural analysis of the CRISPR RAMP domain family member Cas5d. (A, top) Ribbon diagram derived from the X-ray structure of M. succiniciproducens MS0988. α-helices and β-strands are colored red and yellow, respectively. (B) Alignment of MS0988 and T. thermophilus TTP0133 primary sequence and secondary structure diagrams depicting α-helices (red) and β-strands (yellow) derived from pdb and homology modeling by Protein Homology/analogY Recognition Engine (Phyre; http://www.sbg.bio.ic.ac.uk/phyre2) (Kelley and Sternberg 2009). Amino acids 71–103, 196–199, and 221–235 are disordered in the MS0988 structure. Also indicated are sequence identity (*), conservation (:), and partial conservation (.). (C, top) Structural model of T. thermophilus Cas 5d based on submission of the primary sequence of TTP0133 to Phyre.
