1GM5

Structure of RecG bound to three-way DNA junction

Summary for 1GM5

• Entry DOI: 10.2210/pdb1gm5/pdb
• Descriptor: RECG, DNA (5'-(*CP*AP*GP*CP*TP*CP*CP*AP*TP*GP*AP*TP* CP*AP*TP*TP*GP*GP*CP*A)-3'), DNA (5'-(*GP*CP*AP*GP*TP*GP*CP*TP*CP*GP*CP*AP* TP*GP*GP*AP*GP*CP*TP*G)-3'), ... (6 entities in total)
• Functional Keywords: helicase, replication restart
• Biological source: THERMOTOGA MARITIMA
• Total number of polymer chains: 4
• Total formula weight: 105536.48

Authors

Singleton, M.R.,Scaife, S.,Wigley, D.B. (deposition date: 2001-09-11, release date: 2001-10-03, Last modification date: 2024-10-23)

Primary citation

Singleton, M.R.,Scaife, S.,Wigley, D.B.
Structural Analysis of DNA Replication Fork Reversal by Recg
Cell(Cambridge,Mass.), 107:79-, 2001

PubMed Abstract: The stalling of DNA replication forks that occurs as a consequence of encountering DNA damage is a critical problem for cells. RecG protein is involved in the processing of stalled replication forks, and acts by reversing the fork past the damage to create a four-way junction that allows template switching and lesion bypass. We have determined the crystal structure of RecG bound to a DNA substrate that mimics a stalled replication fork. The structure not only reveals the elegant mechanism used by the protein to recognize junctions but has also trapped the protein in the initial stage of fork reversal. We propose a mechanism for how forks are processed by RecG to facilitate replication fork restart. In addition, this structure suggests that the mechanism and function of the two largest helicase superfamilies are distinct.

PubMed: 11595187
DOI: 10.1016/S0092-8674(01)00501-3

Experimental method

X-RAY DIFFRACTION (3.24 Å)