3SPD

Crystal structure of aprataxin ortholog Hnt3 in complex with DNA

Summary for 3SPD

• Entry DOI: 10.2210/pdb3spd/pdb
• Related: 3SP4 3SPL
• Descriptor: Aprataxin-like protein, DNA (5'-D(*TP*AP*TP*TP*CP*CP*GP*AP*TP*AP*GP*TP*GP*AP*C)-3'), DNA (5'-D(*GP*TP*CP*AP*CP*TP*AP*TP*CP*GP*GP*AP*AP*TP*GP*AP*G)-3'), ... (6 entities in total)
• Functional Keywords: hit domain, zinc finger, dna deadenylase, dna binding, hydrolase-dna complex, hydrolase/dna
• Biological source: Schizosaccharomyces pombe (Fission yeast); More
• Cellular location: Nucleus: O74859
• Total number of polymer chains: 8
• Total formula weight: 115901.73

Authors

Gong, Y.,Zhu, D.,Ding, J.,Dou, C.,Ren, X.,Jiang, T.,Wang, D. (deposition date: 2011-07-01, release date: 2011-10-12, Last modification date: 2023-11-01)

Primary citation

Gong, Y.,Zhu, D.,Ding, J.,Dou, C.,Ren, X.,Gu, L.,Jiang, T.,Wang, D.
Crystal structures of aprataxin ortholog Hnt3 reveal the mechanism for reversal of 5'-adenylated DNA
Nat.Struct.Mol.Biol., 18:1297-1299, 2011

PubMed Abstract: Aprataxin is a DNA deadenylase that resolves DNA 5'-AMP termini and reverses abortive DNA ligation. The crystal structures of Schizosaccharomyces pombe aprataxin Hnt3 in its apo form and in complex to dsDNA and dsDNA-AMP reveal how Hnt3 recognizes and processes 5'-adenylated DNA in a structure-specific manner. The bound DNA adopts a 5'-flap conformation that facilitates 5'-AMP access to the active site, where AMP cleavage occurs by a canonical catalytic mechanism.

PubMed: 21984208
DOI: 10.1038/nsmb.2145

Experimental method

X-RAY DIFFRACTION (1.912 Å)