5XEX

Crystal structure of S.aureus PNPase catalytic domain

Summary for 5XEX

• Entry DOI: 10.2210/pdb5xex/pdb
• Descriptor: Polyribonucleotide nucleotidyltransferase, DI(HYDROXYETHYL)ETHER, GLYCEROL, ... (5 entities in total)
• Functional Keywords: polynucleotide phosphorylase, catalytic domain, transferase
• Biological source: Staphylococcus aureus (strain NCTC 8325)
• Cellular location: Cytoplasm : Q2FZ20
• Total number of polymer chains: 6
• Total formula weight: 375254.51

Authors

Wang, X.,Zhang, X.,Zang, J. (deposition date: 2017-04-06, release date: 2017-10-18, Last modification date: 2023-11-22)

Primary citation

Wang, X.,Wang, C.,Wu, M.,Tian, T.,Cheng, T.,Zhang, X.,Zang, J.
Enolase binds to RnpA in competition with PNPase in Staphylococcus aureus
FEBS Lett., 591:3523-3535, 2017

PubMed Abstract: The RNA degradosome of the pathogen Staphylococcus aureus regulates the metabolism of RNA, the expression of virulence factors, and the formation of biofilms. It is composed of the RNases J1/J2, RNase Y, CshA, PNPase, Enolase, Pfk, and a newly identified component, RnpA. However, the function and new partners of RnpA in RNA degradosome remain unknown. Here, we identified PNPase and Enolase as two novel partners for RnpA. Further studies revealed that Enolase interacts with RnpA in competition with PNPase. Enzymatic assays showed that RnpA increases Enolase activity but has no effect on PNPase. These findings provide more information about the functional relationship between RnpA and RNA degradosome.

PubMed: 28960276
DOI: 10.1002/1873-3468.12859

Experimental method

X-RAY DIFFRACTION (2.2 Å)