2B2N

Structure of transcription-repair coupling factor

Summary for 2B2N

• Entry DOI: 10.2210/pdb2b2n/pdb
• Descriptor: Transcription-repair coupling factor, SODIUM ION, O-ACETALDEHYDYL-HEXAETHYLENE GLYCOL, ... (5 entities in total)
• Functional Keywords: x-ray crystallography; strand-specific repair; template strand; rna polymerase; rnap; uvra/b/c repair system, transcription, dna repair
• Biological source: Escherichia coli
• Cellular location: Cytoplasm : P30958
• Total number of polymer chains: 2
• Total formula weight: 79604.81

Authors

Assenmacher, N.,Wenig, K.,Lammens, A.,Hopfner, K.-P. (deposition date: 2005-09-19, release date: 2006-01-24, Last modification date: 2024-02-14)

Primary citation

Assenmacher, N.,Wenig, K.,Lammens, A.,Hopfner, K.-P.
Structural Basis for Transcription-coupled Repair: the N Terminus of Mfd Resembles UvrB with Degenerate ATPase Motifs
J.Mol.Biol., 355:675-683, 2006

PubMed Abstract: 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.

PubMed: 16309703
DOI: 10.1016/j.jmb.2005.10.033

Experimental method

X-RAY DIFFRACTION (2.1 Å)