5c31 | pdb_00005c31

Constitutively active Sin recombinase catalytic domain reveals two rotational intermediates

spinqualitylabelsall models 5c31, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5c31 is a 12 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MSE, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BIN3_STAAU Potential DNA invertase. Publication Abstract from PubMed 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. Snapshots of a molecular swivel in action.,Trejo CS, Rock RS, Stark WM, Boocock MR, Rice PA Nucleic Acids Res. 2018 Jun 1;46(10):5286-5296. doi: 10.1093/nar/gkx1309. PMID:29315406 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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