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1gm5
From Proteopedia
Contents |
STRUCTURE OF RECG BOUND TO THREE-WAY DNA JUNCTION
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.
Structural analysis of DNA replication fork reversal by RecG., Singleton MR, Scaife S, Wigley DB, Cell. 2001 Oct 5;107(1):79-89. PMID:11595187
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
| 1gm5, resolution 3.24Å (). | |||||||||
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| Ligands: | , | ||||||||
| Domains: | RecG_wedge_OBF, HELICc, RecG, DEXHc | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
1GM5 is a 4 chains structure (1 protein chain and 3 nucleic acid chains) of sequences from Thermotoga maritima. Full crystallographic information is available from OCA.
This structure is featured in a topic page entitled RecG Bound to Three-Way DNA Junction.
Additional Resources
For additional information, see: DNA Replication, Repair, and Recombination
Reference
- Singleton MR, Scaife S, Wigley DB. Structural analysis of DNA replication fork reversal by RecG. Cell. 2001 Oct 5;107(1):79-89. PMID:11595187
Page originally seeded by OCA on Mon Feb 16 22:17:57 2009
