1KU5

Crystal Structure of recombinant histone HPhA from hyperthermophilic archaeon Pyrococcus horikoshii OT3

1KU5 の概要

• エントリーDOI: 10.2210/pdb1ku5/pdb
• 分子名称: HPhA, ACETATE ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: histone fold, dna binding protein
• 由来する生物種: Pyrococcus horikoshii
• 細胞内の位置: Cytoplasm (Potential): O74098
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 16037.82

構造登録者

Li, T.,Sun, F.,Ji, X.,Feng, Y.,Rao, Z. (登録日: 2002-01-21, 公開日: 2003-08-26, 最終更新日: 2023-10-25)

主引用文献

Li, T.,Sun, F.,Ji, X.,Feng, Y.,Rao, Z.
Structure based hyperthermostability of archaeal histone HPhA from Pyrococcus horikoshii
J.MOL.BIOL., 325:1031-1037, 2003

PubMed Abstract: The histone protein HPhA from the hyperthermophilic archaeon Pyrococcus horikoshii, shows hyperthermostability, as required for optimal growth of the organism at 95 degrees C. The structure of recombinant P.horikoshii HPhA has been determined to 2.3A resolution by molecular replacement, and refined to R(work) and R(free) values of 20.7% and 27.3%, respectively. The HPhA monomer structure is characterized by the histone fold and assembles into a homodimer like other archaeal histones. There are four anions found in the dimer structure, giving rise to clues as to where DNA might bind. A detailed comparison of four known structures of archaeal histones, which evolve and exist under different temperatures, shows that the thermophilic archaeal histone HPhA has a larger hydrophobic contact area, an increased number of hydrogen bonds and a reduced solvent-accessible area. We also observe a unique network of tyrosine residues located at the crossover point of the two HPhA monomers, which locks them together and stabilizes the dimer. These factors together account for the increased thermal stability.

PubMed: 12527306
DOI: 10.1016/S0022-2836(02)01285-8

実験手法

X-RAY DIFFRACTION (2.3 Å)