2b2n

From Proteopedia

Revision as of 06:24, 21 November 2007

Structure of transcription-repair coupling factor

Overview

The transcription repair coupling factor Mfd removes stalled RNA, polymerase from DNA lesions and links transcription to UvrABC-dependent, nucleotide excision repair in prokaryotes. We report the 2.1A crystal, structure of the UvrA-binding N terminus (residues 1-333) of Escherichia, coli Mfd (Mfd-N). Remarkably, Mfd-N reveals a fold that resembles the, three N-terminal domains of the repair enzyme UvrB. Domain 1A of Mfd, adopts a typical RecA fold, domain 1B matches the damage-binding domain of, the UvrB, and domain 2 highly resembles the implicated UvrA-binding domain, of UvrB. However, Mfd apparently lacks a functional ATP-binding site and, does not contain the DNA damage-binding motifs of UvrB. Thus, our results, suggest that Mfd might form a UvrA recruitment factor at stalled, transcription complexes that architecturally but not catalytically, resembles UvrB.

About this Structure

2B2N is a Single protein structure of sequence from Escherichia coli with NA, SO4 and P4C as ligands. Full crystallographic information is available from OCA.

Reference

Structural basis for transcription-coupled repair: the N terminus of Mfd resembles UvrB with degenerate ATPase motifs., Assenmacher N, Wenig K, Lammens A, Hopfner KP, J Mol Biol. 2006 Jan 27;355(4):675-83. Epub 2005 Nov 8. PMID:16309703

Page seeded by OCA on Wed Nov 21 08:32:13 2007