5C35: Constitutively active Sin recombinase cataltyic domain - T77II100T/Q115R

Members of the serine family of site-specific recombinases exchange DNA strands via 180 degrees rotation about a central protein-protein interface. Modeling of this process has been hampered by the lack of structures in more than one rotational state for any individual serine recombinase. Here we report crystal structures of the catalytic domains of four constitutively active mutants of the serine recombinase Sin, providing snapshots of rotational states not previously visualized for Sin, including two seen in the same crystal. Normal mode analysis predicted that each tetramer's lowest frequency mode (i.e. most accessible large-scale motion) mimics rotation: two protomers rotate as a pair with respect to the other two. Our analyses also suggest that rotation is not a rigid body movement around a single symmetry axis but instead uses multiple pivot points and entails internal motions within each subunit.
PDB ID: 5C35Download
MMDB ID: 145713
PDB Deposition Date: 2015/6/16
Updated in MMDB: 2016/12
Experimental Method:
x-ray diffraction
Resolution: 2.4  Å
Source Organism:
Similar Structures:
Biological Unit for 5C35: tetrameric; determined by author and by software (PISA)
Molecular Components in 5C35
Label Count Molecule
Proteins (4 molecules)
Recombinase SIN
Molecule annotation
Chemicals (4 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB