1jy1: Difference between revisions
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==Overview== | ==Overview== | ||
Tyrosyl-DNA phosphodiesterase (Tdp1) catalyzes the hydrolysis of a | 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== | ==Disease== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Champoux, J | [[Category: Champoux, J J.]] | ||
[[Category: Davies, D | [[Category: Davies, D R.]] | ||
[[Category: Hol, W | [[Category: Hol, W G.J.]] | ||
[[Category: Interthal, H.]] | [[Category: Interthal, H.]] | ||
[[Category: pld superfamily]] | [[Category: pld superfamily]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:28:00 2008'' | ||