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  Common structural features of nucleic acid polymerases

Cramer, P. (2002). Common structural features of nucleic acid polymerases. Bioessays, 24(8), 724-729. doi:10.1002/bies.10127.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0015-86B0-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-C570-2
Genre: Journal Article

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1940903.pdf (Publisher version), 171KB
 
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 Creators:
Cramer, P.1, Author              
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1Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_1863498              

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 Abstract: Structures of multisubunit RNA polymerases strongly differ from the many known structures of single subunit DNA and RNA polymerases. However, in functional complexes of these diverse enzymes, nucleic acids take a similar course through the active center. This finding allows superposition of diverse polymerases and reveals features that are functionally equivalent. The entering DNA duplex is bent by almost 908 with respect to the exiting template–product duplex. At the point of bending, a dramatic twist between subsequent DNA template bases aligns the ‘‘coding‘‘ base with the binding site for the incoming nucleoside triphosphate (NTP). The NTP enters through an opening that is found in all polymerases, and, in most cases, binds between an a-helix and two catalytic metal ions. Subsequent phosphodiester bond formation adds a new base pair to the exiting template–product duplex, which is always bound from the minor groove side. All polymerases may undergo ‘‘induced fit’’ upon nucleic acid binding, but the underlying conformational changes differ.

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Language(s): eng - English
 Dates: 2002-07-232002-08
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1002/bies.10127
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Title: Bioessays
Source Genre: Journal
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Pages: - Volume / Issue: 24 (8) Sequence Number: - Start / End Page: 724 - 729 Identifier: -