2Z7C

Crystal structure of chromatin protein alba from hyperthermophilic archaeon pyrococcus horikoshii

Summary for 2Z7C

• Entry DOI: 10.2210/pdb2z7c/pdb
• Descriptor: DNA/RNA-binding protein Alba, ARGININE (3 entities in total)
• Functional Keywords: alba, dna/rna binding, acetylation, cytoplasm, dna-binding, rna-binding, dna binding protein, rna binding protein
• Biological source: Pyrococcus horikoshii
• Total number of polymer chains: 4
• Total formula weight: 41946.37

Authors

Hada, K.,Nakashima, T.,Osawa, T.,Shimada, H.,Kakuta, Y.,Kimura, M. (deposition date: 2007-08-17, release date: 2008-08-05, Last modification date: 2023-11-01)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)