1qzq

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[[Image:1qzq.gif|left|200px]]
[[Image:1qzq.gif|left|200px]]
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{{Structure
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|PDB= 1qzq |SIZE=350|CAPTION= <scene name='initialview01'>1qzq</scene>, resolution 2.40&Aring;
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The line below this paragraph, containing "STRUCTURE_1qzq", creates the "Structure Box" on the page.
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|GENE= tdp1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_1qzq| PDB=1qzq | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qzq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qzq OCA], [http://www.ebi.ac.uk/pdbsum/1qzq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qzq RCSB]</span>
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'''human Tyrosyl DNA phosphodiesterase'''
'''human Tyrosyl DNA phosphodiesterase'''
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[[Category: Rideout, M C.]]
[[Category: Rideout, M C.]]
[[Category: Staker, B.]]
[[Category: Staker, B.]]
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[[Category: dna repair]]
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[[Category: Dna repair]]
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[[Category: replication]]
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[[Category: Replication]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:54:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:21:17 2008''
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Revision as of 03:54, 3 May 2008

Image:1qzq.gif

Template:STRUCTURE 1qzq

human Tyrosyl DNA phosphodiesterase


Overview

Tyrosyl-DNA phosphodiesterase I (Tdp1) is involved in the repair of DNA lesions created by topoisomerase I in vivo. Tdp1 is a member of the phospholipase D (PLD) superfamily of enzymes and hydrolyzes 3'-phosphotyrosyl bonds to generate 3'-phosphate DNA and free tyrosine in vitro. Here, we use synthetic 3'-(4-nitro)phenyl, 3'-(4-methyl)phenyl, and 3'-tyrosine phosphate oligonucleotides to study human Tdp1. Kinetic analysis of human Tdp1 (hTdp1) shows that the enzyme has nanomolar affinity for all three substrates and the overall in vitro reaction is diffusion-limited. Analysis of active-site mutants using these modified substrates demonstrates that hTdp1 uses an acid/base catalytic mechanism. The results show that histidine 493 serves as the general acid during the initial transesterification, in agreement with hypotheses based on previous crystal structure models. The results also argue that lysine 495 and asparagine 516 participate in the general acid reaction, and the analysis of crystal structures suggests that these residues may function in a proton relay. Together with previous crystal structure data, the new functional data provide a mechanistic understanding of the conserved histidine, lysine and asparagine residues found among all PLD family members.

About this Structure

1QZQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Analysis of human tyrosyl-DNA phosphodiesterase I catalytic residues., Raymond AC, Rideout MC, Staker B, Hjerrild K, Burgin AB Jr, J Mol Biol. 2004 May 14;338(5):895-906. PMID:15111055 Page seeded by OCA on Sat May 3 06:54:00 2008

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