5Y9P

Staphylococcus aureus RNase HII

Summary for 5Y9P

• Entry DOI: 10.2210/pdb5y9p/pdb
• Descriptor: Ribonuclease HII, GLYCEROL (3 entities in total)
• Functional Keywords: endonuclease, hydrolase
• Biological source: Staphylococcus aureus
• Total number of polymer chains: 1
• Total formula weight: 30079.36

Authors

Hang, T.,Wu, M.,Zhang, X. (deposition date: 2017-08-26, release date: 2018-08-01, Last modification date: 2023-11-22)

Primary citation

Hang, T.,Zhang, X.,Wu, M.,Wang, C.,Ling, S.,Xu, L.,Gong, Q.,Tian, C.,Zhang, X.,Zang, J.
Structural insights into a novel functional dimer of Staphylococcus aureus RNase HII
Biochem. Biophys. Res. Commun., 503:1207-1213, 2018

PubMed Abstract: RNase HII exists ubiquitously in organisms and functions as a monomer in prokaryotes. We determined the crystal structure of Staphylococcus aureus RNase HII (Sa-RNase HII), which displays a novel dimer conformation, with the active site of each monomer covered by the other one. Both small-angle X-ray scattering and gel-filtration analysis confirmed that Sa-RNase HII exists as a homodimer in solution. Enzymatic analysis revealed that the "self-inhibited" dimeric form is catalytically active. Furthermore, continuous-wave electron paramagnetic resonance experiments clarified that the Sa-RNase HII dimer undergoes a large conformational change upon substrate binding, but remains a dimer to catalyze the reaction. Our structural and biochemical studies identified a novel functional dimer of Sa-RNase HII with distinct regulation mechanism for its catalytic activity.

PubMed: 30005877
DOI: 10.1016/j.bbrc.2018.07.026

Experimental method

X-RAY DIFFRACTION (2.2 Å)