4APV

The Klebsiella pneumoniae primosomal PriB protein: identification, crystal structure, and ssDNA binding mode

4APV の概要

• エントリーDOI: 10.2210/pdb4apv/pdb
• 分子名称: PRIMOSOMAL REPLICATION PROTEIN N (2 entities in total)
• 機能のキーワード: replication, prib primosome ssdna binding
• 由来する生物種: KLEBSIELLA PNEUMONIAE
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12559.39

構造登録者

Lo, Y.H.,Huang, Y.H.,Hsiao, C.D.,Huang, C.Y. (登録日: 2012-04-06, 公開日: 2012-04-25, 最終更新日: 2024-11-20)

主引用文献

Huang, Y.,Lo, Y.H.,Huang, W.,Huang, C.Y.
Crystal Structure and DNA-Binding Mode of Klebsiella Pneumoniae Primosomal Prib Protein.
Genes Cells, 17:837-, 2012

PubMed Abstract: PriB is a primosomal DNA replication protein required for the re-initiation of replication in bacteria. In this study, we investigated the gene expression of PriB in Klebsiella pneumoniae (KpPriB) and characterized the gene product through crystal structural and functional analyses. Quantitative polymerase chain reaction analysis (Q-PCR) indicated that the 104-aa priB was expressed in K. pneumoniae with a C(T) value of 22.4. The crystal structure of KpPriB (Protein Data Bank entry: 4APV) determined at a resolution of 2.1 Å was similar to that of Escherichia coli PriB (EcPriB). KpPriB formed a single complex with single-stranded DNA (ssDNA) of different lengths, suggesting a highly cooperative process. Structure-based mutational analysis revealed that substitution at K18, F42, R44, W47, K82, K84, or K89 but not R34 in KpPriB had a significant effect on both ssDNA and double-stranded DNA (dsDNA) binding. Based on these findings, the known ssDNA interaction sites of PriB were expanded to include R44 and F42, thus allowing nucleic acids to wrap around the whole PriB protein.

PubMed: 22938024
DOI: 10.1111/GTC.12001

実験手法

X-RAY DIFFRACTION (2.095 Å)