PMID:9757823
| Citation |
Singh, K and Modak, MJ (1998) A unified DNA- and dNTP-binding mode for DNA polymerases. Trends Biochem. Sci. 23:277-81 |
|---|---|
| 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. |
| Links | |
| Keywords |
Binding Sites; DNA/metabolism; DNA Polymerase I/chemistry; DNA Polymerase I/metabolism; DNA Polymerase beta/chemistry; DNA Polymerase beta/metabolism; DNA-Directed DNA Polymerase/chemistry; DNA-Directed DNA Polymerase/metabolism; HIV Reverse Transcriptase/chemistry; HIV Reverse Transcriptase/metabolism; Models, Molecular; Protein Conformation; Taq Polymerase/chemistry; Taq Polymerase/metabolism |
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