PDBsum entry 5y9p

Hydrolase

PDB id: 5y9p

Contents

Protein chain

212 a.a.

Ligands

GOL ×2

Waters ×91

PDB id:

5y9p

Name:

Hydrolase

Title:

Staphylococcus aureus rnase hii

Structure:

Ribonuclease hii. Chain: a. Synonym: rnase hii. Engineered: yes

Source:

Staphylococcus aureus. Organism_taxid: 1280. Gene: rnhb, aym28_06605, aym37_06605, ers072738_01674, ers074020_01342, hmpref3211_01288. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

2.20Å R-factor: 0.238 R-free: 0.282

Authors:

T.Hang,M.Wu,X.Zhang

Key ref:

T.Hang et al. (2018). Structural insights into a novel functional dimer of Staphylococcus aureus RNase HII. Biochem Biophys Res Commun, 503, 1207-1213. PubMed id: 30005877 DOI: 10.1016/j.bbrc.2018.07.026

Date:

26-Aug-17 Release date: 01-Aug-18

Protein chain

Q2FZ38  (RNH2_STAA8) -  Ribonuclease HII from Staphylococcus aureus (strain NCTC 8325 / PS 47)

Seq: 255 a.a.

Struc: 212 a.a.

Enzyme reactions

• Enzyme class: E.C.3.1.26.4 - ribonuclease H.
• Reaction: Endonucleolytic cleavage to 5'-phosphomonoester.

DOI no: 10.1016/j.bbrc.2018.07.026

Biochem Biophys Res Commun 503:1207-1213 (2018)

PubMed id: 30005877

Structural insights into a novel functional dimer of Staphylococcus aureus RNase HII.

T.Hang, X.Zhang, M.Wu, C.Wang, S.Ling, L.Xu, Q.Gong, C.Tian, X.Zhang, J.Zang.

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.