2v1c

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|PDB= 2v1c |SIZE=350|CAPTION= <scene name='initialview01'>2v1c</scene>, resolution 3.80&Aring;
|PDB= 2v1c |SIZE=350|CAPTION= <scene name='initialview01'>2v1c</scene>, resolution 3.80&Aring;
|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+C'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+C'>AC1</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2v1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v1c OCA], [http://www.ebi.ac.uk/pdbsum/2v1c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2v1c RCSB]</span>
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[[Category: Mcsweeney, S.]]
[[Category: Mcsweeney, S.]]
[[Category: Timmins, J.]]
[[Category: Timmins, J.]]
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[[Category: ZN]]
 
[[Category: deinococcus radioduran]]
[[Category: deinococcus radioduran]]
[[Category: dna binding]]
[[Category: dna binding]]
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[[Category: zinc-finger]]
[[Category: zinc-finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:42:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:07:23 2008''

Revision as of 02:07, 31 March 2008

Image:2v1c.jpg


PDB ID 2v1c

Drag the structure with the mouse to rotate
, resolution 3.80Å
Sites:
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE AND MUTATIONAL STUDY OF RECOR PROVIDE INSIGHT INTO ITS ROLE IN DNA REPAIR


Overview

The crystal structure of the complex formed between Deinococcus radiodurans RecR and RecO (drRecOR) has been determined. In accordance with previous biochemical characterisation, the drRecOR complex displays a RecR:RecO molecular ratio of 2:1. The biologically relevant drRecOR entity consists of a heterohexamer in the form of two drRecO molecules positioned on either side of the tetrameric ring of drRecR, with their OB (oligonucleotide/oligosaccharide-binding) domains pointing towards the interior of the ring. Mutagenesis studies validated the protein-protein interactions observed in the crystal structure and allowed mapping of the residues in the drRecOR complex required for DNA binding. Furthermore, the preferred DNA substrate of drRecOR was identified as being 3'-overhanging DNA, as encountered at ssDNA-dsDNA junctions. Together these results suggest a possible mechanism for drRecOR recognition of stalled replication forks.

About this Structure

2V1C is a Protein complex structure of sequences from Deinococcus radiodurans. Full crystallographic information is available from OCA.

Reference

Crystal structure and mutational study of RecOR provide insight into its mode of DNA binding., Timmins J, Leiros I, McSweeney S, EMBO J. 2007 Jul 11;26(13):3260-71. Epub 2007 Jun 21. PMID:17581636

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