1gm5

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{{STRUCTURE_1gm5| PDB=1gm5 | SCENE= }}
{{STRUCTURE_1gm5| PDB=1gm5 | SCENE= }}
===STRUCTURE OF RECG BOUND TO THREE-WAY DNA JUNCTION===
===STRUCTURE OF RECG BOUND TO THREE-WAY DNA JUNCTION===
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{{ABSTRACT_PUBMED_11595187}}
{{ABSTRACT_PUBMED_11595187}}
==About this Structure==
==About this Structure==
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[[1gm5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GM5 OCA].
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[[1gm5]] is a 4 chain structure of [[RecG Bound to Three-Way DNA Junction]] with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GM5 OCA].
==See Also==
==See Also==
*[[RecG Bound to Three-Way DNA Junction|RecG Bound to Three-Way DNA Junction]]
*[[RecG Bound to Three-Way DNA Junction|RecG Bound to Three-Way DNA Junction]]
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*[[User:Wayne Decatur/Plant Viral Protein p19 Suppression of RNA Silencing|User:Wayne Decatur/Plant Viral Protein p19 Suppression of RNA Silencing]]
 
==Reference==
==Reference==

Revision as of 08:53, 29 July 2012


PDB ID 1gm5

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1gm5, resolution 3.24Å ()
Ligands: ,
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



Contents

STRUCTURE OF RECG BOUND TO THREE-WAY DNA JUNCTION

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.

About this Structure

1gm5 is a 4 chain structure of RecG Bound to Three-Way DNA Junction with sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

See Also

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

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