1i4v

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SOLUTION STRUCTURE OF THE UMUD' HOMODIMER

Overview

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.

About this Structure

1I4V is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Converting a DNA damage checkpoint effector (UmuD2C) into a lesion bypass polymerase (UmuD'2C)., Ferentz AE, Walker GC, Wagner G, EMBO J. 2001 Aug 1;20(15):4287-98. PMID:11483531

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