1I4V

SOLUTION STRUCTURE OF THE UMUD' HOMODIMER

Summary for 1I4V

• Entry DOI: 10.2210/pdb1i4v/pdb
• NMR Information: BMRB: 5022
• Descriptor: UMUD' PROTEIN (1 entity in total)
• Functional Keywords: sos response, sos mutagenesis, dna repair, dna polymerase v, dna polymerase accessory protein, lexa repressor, lambda ci, signal peptidase, serine-lysine dyad, autocatalytic cleavage, serine protease, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 24617.97

Authors

Ferentz, A.E.,Walker, G.C.,Wagner, G. (deposition date: 2001-02-23, release date: 2001-08-22, Last modification date: 2024-05-22)

Primary citation

Ferentz, A.E.,Walker, G.C.,Wagner, G.
Converting a DNA damage checkpoint effector (UmuD2C) into a lesion bypass polymerase (UmuD'2C).
EMBO J., 20:4287-4298, 2001

PubMed Abstract: During the SOS response of Escherichia coli to DNA damage, the umuDC operon is induced, producing the trimeric protein complexes UmuD2C, a DNA damage checkpoint effector, and UmuD'2C (DNA polymerase V), which carries out translesion synthesis, the basis of 'SOS mutagenesis'. UmuD'2, the homodimeric component of DNA pol V, is produced from UmuD by RecA-facilitated self-cleavage, which removes the 24 N-terminal residues of UmuD. We report the solution structure of UmuD'2 (PDB ID 1I4V) and interactions within UmuD'-UmuD, a heterodimer inactive in translesion synthesis. The overall shape of UmuD'2 in solution differs substantially from the previously reported crystal structure, even though the topologies of the two structures are quite similar. Most significantly, the active site residues S60 and K97 do not point directly at one another in solution as they do in the crystal, suggesting that self-cleavage of UmuD might require RecA to assemble the active site. Structural differences between UmuD'2 and UmuD'- UmuD suggest that UmuD'2C and UmuD2C might achieve their different biological activities through distinct interactions with RecA and DNA pol III.

PubMed: 11483531
DOI: 10.1093/emboj/20.15.4287

Experimental method

SOLUTION NMR