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| - | [[Image:1ois.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1ois| PDB=1ois | SCENE= }} | | {{STRUCTURE_1ois| PDB=1ois | SCENE= }} |
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| - | '''YEAST DNA TOPOISOMERASE I, N-TERMINAL FRAGMENT'''
| + | ===YEAST DNA TOPOISOMERASE I, N-TERMINAL FRAGMENT=== |
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| - | ==Overview==
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| - | BACKGROUND: Type I DNA topoisomerases, divided mechanistically into two subfamilies, are ubiquitous enzymes that participate in replication and transcription. In addition to its role in these fundamental processes, the biological importance of eukaryotic DNA topoisomerase I is underscored by its identification as the target of the antitumor alkaloid camptothecin. An understanding of the mechanism of catalysis and interactions with camptothecin and other drugs has been hampered by a lack of detailed structural information. RESULTS: The three-dimensional structure of a 26 kDA fragment (residues 135 to about 363) of Saccharomyces cerevisiae DNA topoisomerase I has been determined at 1.9 A resolution. The fragment has a novel architecture comprising a concave platform and a pair of outlying V-shaped helices. Photocrosslinking and protein footprinting experiments show that the positively charged concave surface and the junction region of the V-shaped pair of helices contact DNA in the enzyme-DNA complex. CONCLUSIONS: Crystallographic, biochemical and genetic data indicate that this 26 kDa fragment of yeast DNA topoisomerase I is involved in complex formation between the enzyme and DNA, and probably also in camptothecin-enzyme-DNA ternary complex formation. A molecular model for protein-DNA interaction based on these data is proposed. The bipartite DNA-binding regions of the 26 kDa fragment may enable eukaryotic DNA topoisomerase I to adapt to sequence-dependent structural variations in its DNA substrates.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8747458}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8747458 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8747458}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Isomerase]] | | [[Category: Isomerase]] |
| | [[Category: Topoisomerase]] | | [[Category: Topoisomerase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:54:06 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:21:36 2008'' |
Revision as of 03:21, 29 July 2008
Template:STRUCTURE 1ois
YEAST DNA TOPOISOMERASE I, N-TERMINAL FRAGMENT
Template:ABSTRACT PUBMED 8747458
About this Structure
1OIS is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
A 26 kDa yeast DNA topoisomerase I fragment: crystallographic structure and mechanistic implications., Lue N, Sharma A, Mondragon A, Wang JC, Structure. 1995 Dec 15;3(12):1315-22. PMID:8747458
Page seeded by OCA on Tue Jul 29 06:21:36 2008
