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  A helical arch allowing single-stranded DNA to thread through T5 5'-exonuclease

Ceska, T. A., Sayers, J. R., Stier, G., & Suck, D. (1996). A helical arch allowing single-stranded DNA to thread through T5 5'-exonuclease. Nature, 382(6586), 90-93. doi:10.1038/382090a0.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-A6B9-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-AC3E-1
Genre: Journal Article

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Nature_382_1996_90.pdf (Any fulltext), 2MB
 
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Ceska, T. A., Author
Sayers, J. R., Author
Stier, Gunter1, Author              
Suck, Dietrich, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: THE 5'-exonucleases are enzymes that are essential for DNA replication and repair. As well as their exonucleolytic action, removing nucleotides from the 5'-end of nucleic acid molecules such as Okazaki fragments, many 5'-3'-exonucleases have been shown to possess endonucleolytic activities. T5 5'-3'-exonuclease shares many similarities with the amino terminal of eubacterial DNA polymerases, although, unlike eubacteria, phages such as T5, T4 and T7 express polymerase and 5'-exonuclease proteins from separate genes. Here we report the 2.5-A crystal structure of the phage T5 5'-exonuclease, which reveals a helical arch for binding DNA. We propose a model consistent with a threading mechanism in which single-stranded DNA could slide through the arch, which is formed by two helices, one containing positively charged, and the other hydrophobic, residues. The active site is at the base of the arch, and contains two metal-binding sites.

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Language(s): eng - English
 Dates: 1996-02-271996-05-211996-07-04
 Publication Status: Published in print
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 664779
DOI: 10.1038/382090a0
URI: https://www.ncbi.nlm.nih.gov/pubmed/8657312
Other: 7344
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Title: Nature
  Abbreviation : Nature
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 382 (6586) Sequence Number: - Start / End Page: 90 - 93 Identifier: ISSN: 0028-0836
CoNE: https://pure.mpg.de/cone/journals/resource/954925427238