1gm5 | pdb_00001gm5

STRUCTURE OF RECG BOUND TO THREE-WAY DNA JUNCTION

spinqualitylabelsall models 1gm5, resolution 3.24Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1gm5 is a 4 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, MG Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. See Also Helicase RecG Bound to Three-Way DNA Junction

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