2VLD

crystal structure of a repair endonuclease from Pyrococcus abyssi

Summary for 2VLD

• Entry DOI: 10.2210/pdb2vld/pdb
• Descriptor: Endonuclease NucS (2 entities in total)
• Functional Keywords: endonuclease, hydrolase
• Biological source: Pyrococcus abyssi
• Total number of polymer chains: 2
• Total formula weight: 58303.80

Authors

Ren, B.,Kuhn, J.,Meslet-Cladiere, L.,Briffotaux, J.,Norais, C.,Lavigne, R.,Flament, D.,Ladenstein, R.,Myllykallio, H. (deposition date: 2008-01-14, release date: 2009-05-19, Last modification date: 2024-10-16)

Primary citation

Ren, B.,Kuhn, J.,Meslet-Cladiere, L.,Briffotaux, J.,Norais, C.,Lavigne, R.,Flament, D.,Ladenstein, R.,Myllykallio, H.
Structure and function of a novel endonuclease acting on branched DNA substrates.
EMBO J., 28:2479-2489, 2009

PubMed Abstract: We show that Pyrococcus abyssi PAB2263 (dubbed NucS (nuclease for ss DNA) is a novel archaeal endonuclease that interacts with the replication clamp PCNA. Structural determination of P. abyssi NucS revealed a two-domain dumbbell-like structure that in overall does not resemble any known protein structure. Biochemical and structural studies indicate that NucS orthologues use a non-catalytic ssDNA-binding domain to regulate the cleavage activity at another site, thus resulting into the specific cleavage at double-stranded DNA (dsDNA)/ssDNA junctions on branched DNA substrates. Both 3' and 5' extremities of the ssDNA can be cleaved at the nuclease channel that is too narrow to accommodate duplex DNA. Altogether, our data suggest that NucS proteins constitute a new family of structure-specific DNA endonucleases that are widely distributed in archaea and in bacteria, including Mycobacterium tuberculosis.

PubMed: 19609302
DOI: 10.1038/emboj.2009.192

Experimental method

X-RAY DIFFRACTION (2.6 Å)