2Z7C

Crystal structure of chromatin protein alba from hyperthermophilic archaeon pyrococcus horikoshii

2Z7C の概要

• エントリーDOI: 10.2210/pdb2z7c/pdb
• 分子名称: DNA/RNA-binding protein Alba, ARGININE (3 entities in total)
• 機能のキーワード: alba, dna/rna binding, acetylation, cytoplasm, dna-binding, rna-binding, dna binding protein, rna binding protein
• 由来する生物種: Pyrococcus horikoshii
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 41946.37

構造登録者

Hada, K.,Nakashima, T.,Osawa, T.,Shimada, H.,Kakuta, Y.,Kimura, M. (登録日: 2007-08-17, 公開日: 2008-08-05, 最終更新日: 2023-11-01)

主引用文献

Hada, K.,Nakashima, T.,Osawa, T.,Shimada, H.,Kakuta, Y.,Kimura, M.
Crystal structure and functional analysis of an archaeal chromatin protein Alba from the hyperthermophilic archaeon Pyrococcus horikoshii OT3.
Biosci.Biotechnol.Biochem., 72:749-758, 2008

PubMed Abstract: The crystal structure of the Alba protein (PhoAlba) from a hyperthermophilic archaeon, Pyrococcus horikoshii OT3, was determined at a resolution of 2.8 A. PhoAlba structurally belongs to the alpha/beta proteins and is similar not only to archaeal homologues but also to RNA-binding proteins, including the C-terminal half of initiation factor 3 (IF3-C) from Bacillus stearothermophilus, an Esherichia coli protein implicated in cell division (Yhhp), and an Arabidopsis protein of unknown function. We found by gel shift assay that PhoAlba interacts with both ribonuclease P (RNase P) RNA (PhopRNA) and precursor-tRNA(Tyr) (pre-tRNA(Tyr)) in P. horikoshii. However, the addition of PhoAlba to reconstituted particles composed of PhopRNA and four or five protein subunits had little influence on either the pre-tRNA processing activity or the optimum temperature for the processing activity. These results suggest that PhoAlba contributes little to the catalytic activity of P. horikoshii RNase P.

PubMed: 18323660
DOI: 10.1271/bbb.70639

実験手法

X-RAY DIFFRACTION (2.8 Å)