1I4V

SOLUTION STRUCTURE OF THE UMUD' HOMODIMER

1I4V の概要

• エントリーDOI: 10.2210/pdb1i4v/pdb
• NMR情報: BMRB: 5022
• 分子名称: UMUD' PROTEIN (1 entity in total)
• 機能のキーワード: 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
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24617.97

構造登録者

Ferentz, A.E.,Walker, G.C.,Wagner, G. (登録日: 2001-02-23, 公開日: 2001-08-22, 最終更新日: 2024-05-22)

主引用文献

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

実験手法

SOLUTION NMR