4EOG

Crystal structure of Csx1 of Pyrococcus furiosus

4EOG の概要

• エントリーDOI: 10.2210/pdb4eog/pdb
• 分子名称: Putative uncharacterized protein, ZINC ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: beta-hairpin, nucleic acid binding protein, rna binding, dna binding protein
• 由来する生物種: Pyrococcus furiosus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 56962.08

構造登録者

Kim, Y.K.,Oh, B.H. (登録日: 2012-04-14, 公開日: 2013-01-02, 最終更新日: 2024-10-09)

主引用文献

Kim, Y.K.,Kim, Y.G.,Oh, B.H.
Crystal structure and nucleic acid-binding activity of the CRISPR-associated protein Csx1 of Pyrococcus furiosus.
Proteins, 81:261-270, 2013

PubMed Abstract: In many prokaryotic organisms, chromosomal loci known as clustered regularly interspaced short palindromic repeats (CRISPRs) and CRISPR-associated (CAS) genes comprise an acquired immune defense system against invading phages and plasmids. Although many different Cas protein families have been identified, the exact biochemical functions of most of their constituents remain to be determined. In this study, we report the crystal structure of PF1127, a Cas protein of Pyrococcus furiosus DSM 3638 that is composed of 480 amino acids and belongs to the Csx1 family. The C-terminal domain of PF1127 has a unique β-hairpin structure that protrudes out of an α-helix and contains several positively charged residues. We demonstrate that PF1127 binds double-stranded DNA and RNA and that this activity requires an intact β-hairpin and involve the homodimerization of the protein. In contrast, another Csx1 protein from Sulfolobus solfataricus P2 that is composed of 377 amino acids does not have the β-hairpin structure and exhibits no DNA-binding properties under the same experimental conditions. Notably, the C-terminal domain of these two Csx1 proteins is greatly diversified, in contrast to the conserved N-terminal domain, which appears to play a common role in the homodimerization of the protein. Thus, although P. furiosus Csx1 is identified as a nucleic acid-binding protein, other Csx1 proteins are predicted to exhibit different individual biochemical activities.

PubMed: 22987782
DOI: 10.1002/prot.24183

実験手法

X-RAY DIFFRACTION (2.3 Å)