5yjj

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Crystal structure of PNPase from Staphylococcus epidermidis

Structural highlights

5yjj is a 6 chain structure with sequence from Staphylococcus epidermidis ATCC 12228. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:MG, PO4
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PNP_STAES Involved in mRNA degradation. Catalyzes the phosphorolysis of single-stranded polyribonucleotides processively in the 3'- to 5'-direction.

Publication Abstract from PubMed

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.

Characterization of Staphylococcus epidermidis Polynucleotide phosphorylase and its interactions with ribonucleases RNase J1 and RNase J2.,Raj R, Mitra S, Gopal B Biochem Biophys Res Commun. 2018 Jan 8;495(2):2078-2084. doi:, 10.1016/j.bbrc.2017.12.056. Epub 2017 Dec 11. PMID:29242153[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
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A type III-A CRISPR-Cas system employs degradosome nucleases to ensure robust immunity.
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See Also

References

  1. ↑ 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. 2018 Jan 8;495(2):2078-2084. doi:, 10.1016/j.bbrc.2017.12.056. Epub 2017 Dec 11. PMID:29242153 doi:http://dx.doi.org/10.1016/j.bbrc.2017.12.056

Contents


PDB ID 5yjj

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