1a36
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(New page: 200px<br /> <applet load="1a36" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a36, resolution 2.800Å" /> '''TOPOISOMERASE I/DN...)
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Revision as of 13:48, 12 November 2007
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TOPOISOMERASE I/DNA COMPLEX
Contents |
Overview
The three-dimensional structure of a 70-kilodalton amino terminally, truncated form of human topoisomerase I in complex with a 22-base pair, duplex oligonucleotide, determined to a resolution of 2.8 angstroms, reveals all of the structural elements of the enzyme that contact DNA. The, linker region that connects the central core of the enzyme to the, carboxyl-terminal domain assumes a coiled-coil configuration and protrudes, away from the remainder of the enzyme. The positively charged DNA-proximal, surface of the linker makes only a few contacts with the DNA downstream of, the cleavage site. In combination with the crystal structures of the, reconstituted human topoisomerase I before and after DNA cleavage, this, information suggests which amino acid residues are involved in catalyzing, phosphodiester bond breakage and religation. The structures also lead to, the proposal that the topoisomerization step occurs by a mechanism termed, "controlled rotation."
Disease
Known disease associated with this structure: DNA topoisomerase I, camptothecin-resistant OMIM:[126420]
About this Structure
1A36 is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 1A36 with [Topoisomerases]. Active as DNA topoisomerase, with EC number 5.99.1.2 Full crystallographic information is available from OCA.
Reference
A model for the mechanism of human topoisomerase I., Stewart L, Redinbo MR, Qiu X, Hol WG, Champoux JJ, Science. 1998 Mar 6;279(5356):1534-41. PMID:9488652
Page seeded by OCA on Mon Nov 12 15:54:56 2007
