ø29 DNA polymerase residue Lys383, invariant at motif B of DNA-dependent polymerases, is involved in dNTP binding.

doi:10.1006/jmbi.1997.1053

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Article

ø29 DNA polymerase residue Lys383, invariant at motif B of DNA-dependent polymerases, is involved in dNTP binding.

Journal of molecular biology - 13 Jun 1997

Saturno J, Lázaro J M, Esteban F J, Blanco L, Salas M

Abstract excerpt

Bacteriophage ø29 DNA polymerase shares with other DNA-dependent DNA polymerases several regions of amino acid homology along the primary structure. Among them, motif B, characterized by the consensus +x3Kx(6-7)YG (+ being a positively charged amino acid), appears to be specifically conserved in...

Topics

Amino Acid Sequence
Bacillus Phages
Binding Sites
DNA Primers
DNA Replication
DNA-Directed DNA Polymerase
Deoxyribonucleotides
Lysine
Magnesium
Manganese
Molecular Sequence Data
Mutation
Nucleotides
Sequence Alignment
Sequence Homology, Amino Acid
Templates, Genetic

Source

Open in PubMed

Identifiers

PMID: 9199402
DOI: 10.1006/jmbi.1997.1053

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-9199402-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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