5YJJ

Crystal structure of PNPase from Staphylococcus epidermidis

Summary for 5YJJ

• Entry DOI: 10.2210/pdb5yjj/pdb
• Descriptor: Polyribonucleotide nucleotidyltransferase, PHOSPHATE ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: polynucleotidyl phosphorylase, rna degradation, polyadenylation, cytosolic protein
• Biological source: Staphylococcus epidermidis (strain ATCC 12228)
• Cellular location: Cytoplasm : Q8CST1
• Total number of polymer chains: 6
• Total formula weight: 474322.66

Authors

Raj, R.,Gopal, B. (deposition date: 2017-10-10, release date: 2018-01-31, Last modification date: 2023-11-22)

Primary citation

Raj, R.,Mitra, S.,Gopal, B.
Characterization of Staphylococcus epidermidis Polynucleotide phosphorylase and its interactions with ribonucleases RNase J1 and RNase J2.
Biochem. Biophys. Res. Commun., 495:2078-2084, 2018

PubMed Abstract: Polynucleotide phosphorylase catalyzes both 3'-5' exoribonuclease and polyadenylation reactions. The crystal structure of Staphylococcus epidermidis PNPase revealed a bound phosphate in the PH2 domain of each protomer coordinated by three adjacent serine residues. Mutational analysis suggests that phosphate coordination by these serine residues is essential to maintain the catalytic center in an active conformation. We note that PNPase forms a complex with RNase J1 and RNase J2 without substantially altering either exo-ribonuclease or polyadenylation activity of this enzyme. This decoupling of catalytic activity from protein-protein interactions suggests that association of these endo- or exo-ribonucleases with PNPase could be more relevant for cellular localization or concerted targeting of structured RNA for recycling.

PubMed: 29242153
DOI: 10.1016/j.bbrc.2017.12.056

Experimental method

X-RAY DIFFRACTION (2.2 Å)