Structural insights into the conformational change of Staphylococcus aureus NreA at C-terminus

Lancine Sangare; Wanbiao Chen; Chengliang Wang; Xiaobao Chen; Minhao Wu; Xuan Zhang; Jianye Zang

doi:10.1007/s10529-020-02807-2

Structural insights into the conformational change of Staphylococcus aureus NreA at C-terminus

Biotechnol Lett. 2020 May;42(5):787-795. doi: 10.1007/s10529-020-02807-2. Epub 2020 Jan 22.

Authors

Lancine Sangare^{1

2

3}, Wanbiao Chen^{1

2}, Chengliang Wang^{1

2}, Xiaobao Chen^{1

2}, Minhao Wu^{1

2}, Xuan Zhang^{1

2}, Jianye Zang^{4

5}

Affiliations

¹ Hefei National Laboratory for Physical Sciences at Microscale, CAS Center for Excellence in Biomacromolecules, Collaborative Innovation Center of Chemistry for Life Sciences, and School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, 230026, Anhui, China.
² Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, 230026, Anhui, China.
³ Institute Superior Agronomic and Veterinary of Faranah, 131, Faranah, Guinea.
⁴ Hefei National Laboratory for Physical Sciences at Microscale, CAS Center for Excellence in Biomacromolecules, Collaborative Innovation Center of Chemistry for Life Sciences, and School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, 230026, Anhui, China. zangjy@ustc.edu.cn.
⁵ Key Laboratory of Structural Biology, Chinese Academy of Sciences, Hefei, 230026, Anhui, China. zangjy@ustc.edu.cn.

PMID: 31970556
DOI: 10.1007/s10529-020-02807-2

Abstract

Staphylococcus aureus is an anaerobic facultative microorganism that features the NreABC system for nitrate respiration. NreB is the sensor histidine kinase that phosphorylates the response regulator NreC to stimulate the expression of target genes. NreA is a nitrate sensor which dissociates from NreB in the present of nitrate and relieves its inhibition on NreB. However, the molecular basis of how NreA regulate NreB remains unknown. In this study, we determined the crystal structures of nitrate-bound NreA from S. aureus (SaNreA/NO₃^-) and its apoNreA-like mutant SaNreAY^94A in complex with ethanediol (SaNreA^Y94A/EDO). Structural comparison reveals that the C-terminal loop in SaNreA/NO₃^- rearranges to an α-helix (α7) in SaNreA^Y94A/EDO, which converts an acidic pocket on the surface to a positively charged region. This conformational change of SaNreA C-terminus might play a role in SaNreB binding.

Keywords: Crystal structure; GAF domain; NreABC system; Staphylococcus aureus.

MeSH terms

Bacterial Proteins / chemistry*
Bacterial Proteins / genetics*
Bacterial Proteins / metabolism
Cloning, Molecular
Crystallography, X-Ray
Histidine Kinase / chemistry*
Histidine Kinase / genetics*
Histidine Kinase / metabolism
Models, Molecular
Mutation
Nitrates / metabolism*
Protein Binding
Protein Conformation
Protein Domains
Staphylococcus aureus / chemistry
Staphylococcus aureus / metabolism*

Substances

Bacterial Proteins
Nitrates
Histidine Kinase