5FBM

Crystal Structure of Histone Like Protein (HLP) from Streptococcus mutans Refined to 1.9 A Resolution

5FBM の概要

• エントリーDOI: 10.2210/pdb5fbm/pdb
• 分子名称: DNA-binding protein HU (2 entities in total)
• 機能のキーワード: histone-like protein, dna binding, dimerization, dna binding protein
• 由来する生物種: Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21658.84

構造登録者

Lovell, S.,Battaile, K.P.,Mehzabeen, N.,O'Neil, P.,Biswas, I. (登録日: 2015-12-14, 公開日: 2016-04-06, 最終更新日: 2023-09-27)

主引用文献

O'Neil, P.,Lovell, S.,Mehzabeen, N.,Battaile, K.,Biswas, I.
Crystal structure of histone-like protein from Streptococcus mutans refined to 1.9 angstrom resolution.
Acta Crystallogr F Struct Biol Commun, 72:257-262, 2016

PubMed Abstract: Nucleoid-associated proteins (NAPs) in prokaryotes play an important architectural role in DNA bending, supercoiling and DNA compaction. In addition to architectural roles, some NAPs also play regulatory roles in DNA replication and repair, and act as global transcriptional regulators in many bacteria. Bacteria encode multiple NAPs and some of them are even essential for survival. Streptococcus mutans, a dental pathogen, encodes one such essential NAP called histone-like protein (HLP). Here, the three-dimensional structure of S. mutans HLP has been determined to 1.9 Å resolution. The HLP structure is a dimer and shares a high degree of similarity with other bacterial NAPs, including HU. Since HLPs are essential for the survival of pathogenic streptococci, this structure determination is potentially beneficial for future drug development against these pathogens.

PubMed: 27050257
DOI: 10.1107/S2053230X1600217X

実験手法

X-RAY DIFFRACTION (1.9 Å)