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Trends Biochem Sci. 1998 Aug;23(8):277-81.

A unified DNA- and dNTP-binding mode for DNA polymerases.

Author information

1
Dept of Biochemistry and Molecular Biology, UMD-New Jersey Medical School, Newark 07103, USA.

Abstract

Crystal structures of various DNA polymerases show a common structural topology that resembles a right hand and has distinct finger, palm and thumb subdomains. Early models of the klenow fragment (KF) of Escherichia coli polymerase I showed DNA entering a large cleft that faces the palm subdomain where the catalytic site is situated1,2. However, subsequent resolution of the structures of HIV-1 reverse transcriptase, KF and polymerase beta (pol beta) bound to DNA3-5 yielded conflicting data that suggested a different orientation for DNA bound to pol beta compared with DNA bound to other polymerases. The debate, on the correct orientation of the template-primer DNA, that followed failed to reach a consensus. Using an alternative superposition scheme, we now provide convincing evidence for a common DNA-binding mode that is applicable to all polymerases, including pol beta.

PMID:
9757823
DOI:
10.1016/s0968-0004(98)01250-x
[Indexed for MEDLINE]

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