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Article

Aromatic residues in the oligonucleotide binding domain are essential to the function of the single-stranded DNA binding protein of Helicobacter pylori.

Journal of bioscience and bioengineering - 1 Jan 2025

Lee Mon-Juan, Huang Li-Kun, Huang Wen-Hsin, Chan Po-Yu, Yang Zi-Sin, Chien Ching-Ming, Chieng Ching-Chang, Huang Haimei

Abstract excerpt

Single-stranded DNA-binding protein (SSB) is essential to DNA replication, DNA repair, and homologous genetic recombination. Our previous study on the crystal structure of a C-terminally truncated SSB from Helicobacter pylori, HpSSBc, in complex with single-stranded DNA (ssDNA) suggests that several aromatic residues, including Phe37, Phe50, Phe56, and Trp84, were involved in ssDNA binding. To investigate the...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 39490297
DOI: 10.1016/j.jbiosc.2024.09.003

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