1vcc
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(New page: 200px<br /><applet load="1vcc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vcc, resolution 1.6Å" /> '''AMINO TERMINAL 9KDA D...)
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Revision as of 02:27, 21 November 2007
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AMINO TERMINAL 9KDA DOMAIN OF VACCINIA VIRUS DNA TOPOISOMERASE I RESIDUES 1-77, EXPERIMENTAL ELECTRON DENSITY FOR RESIDUES 1-77
Overview
BACKGROUND: Vaccinia virus, a cytoplasmically-replicating poxvirus, encodes a type I DNA topoisomerase that is biochemically similar to, eukaryotic-like DNA topoisomerases I, and which has been widely studied as, a model topoisomerase. It is the smallest topoisomerase known and is, unusual in that it is resistant to the potent chemotherapeutic agent, camptothecin. RESULTS: The crystal structure of a 9 kDa amino-terminal, fragment of vaccinia virus DNA topoisomerase I has been determined at 1.6, A resolution. The fragment forms a five-stranded, antiparallel beta-sheet, with two short alpha-helices and connecting loops. Residues that are, conserved between all eukaryotic-like type I topoisomerases are not, clustered in particular regions of the structure. CONCLUSIONS: This is the, first atomic structure of any region of a eukaryotic-like DNA, topoisomerase I. It has provided insights into the structural bases of the, phenotypes of some single-site mutants of the intact topoisomerase. The, structure has enabled us to study the interactions within a well-folded, protein fragment and the camptothecin resistance of the viral, topoisomerase.
About this Structure
1VCC is a Single protein structure of sequence from Vaccinia virus. Active as DNA topoisomerase, with EC number 5.99.1.2 Full crystallographic information is available from OCA.
Reference
Crystal structure of the amino-terminal fragment of vaccinia virus DNA topoisomerase I at 1.6 A resolution., Sharma A, Hanai R, Mondragon A, Structure. 1994 Aug 15;2(8):767-77. PMID:7994576
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