1jy1
From Proteopedia
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CRYSTAL STRUCTURE OF HUMAN TYROSYL-DNA PHOSPHODIESTERASE (TDP1)
Contents |
Overview
Tyrosyl-DNA phosphodiesterase (Tdp1) catalyzes the hydrolysis of a, phosphodiester bond between a tyrosine residue and a DNA 3' phosphate. The, enzyme appears to be responsible for repairing the unique protein-DNA, linkage that occurs when eukaryotic topoisomerase I becomes stalled on the, DNA in the cell. The 1.69 A crystal structure reveals that human Tdp1 is a, monomer composed of two similar domains that are related by a, pseudo-2-fold axis of symmetry. Each domain contributes conserved, histidine, lysine, and asparagine residues to form a single active site., The structure of Tdp1 confirms that the protein has many similarities to, the members of the phospholipase D (PLD) superfamily and indicates a, similar catalytic mechanism. The structure also suggests how the unusual, protein-DNA substrate binds and provides insights about the nature of the, substrate in vivo.
Disease
Known disease associated with this structure: Spinocerebellar ataxia, autosomal recessive with axonal neuropathy OMIM:[607198]
About this Structure
1JY1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The crystal structure of human tyrosyl-DNA phosphodiesterase, Tdp1., Davies DR, Interthal H, Champoux JJ, Hol WG, Structure. 2002 Feb;10(2):237-48. PMID:11839309
Page seeded by OCA on Fri Feb 15 16:10:18 2008
