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Reversible domain closure modulates GlnBP ligand binding affinity
Chen, Qun1; Li, Fang1; Zuo, Xiaobing2; Chen, Jin3; Qin, Peiwu1; Wang, Chuhui1; Xu, Jin4; Yang, Danyu4; Xing, Baogang5; Liu, Ying6; Jia, Peng6; Li, Linling7; Yang, Chengming5; Yu, Dongmei8
2022-04-01
Source PublicationPLoS ONE
ISSN1932-6203
Volume17Issue:4 April
Abstract

Glutamine binding protein (GlnBP) is an Escherichia Coli periplasmic binding protein, which binds and carries glutamine to the inner membrane ATP-binding cassette (ABC) transporter. GlnBP binds the ligand with affinity around 0.1μM measured by isothermal titration calorimetry (ITC) and ligand binding stabilizes protein structure shown by its increase in thermodynamic stability. However, the molecular determinant of GlnBP ligand binding is not known. Electrostatic and hydrophobic interaction between GlnBP and glutamine are critical factors. We propose that the freedome of closure movement is also vital for ligand binding. In order to approve this hypothesis, we generate a series of mutants with different linker length that has different magnitude of domain closure. Mutants show different ligand binding affinity, which indicates that the propensity of domain closure determines the ligand binding affinity. Ligand binding triggers gradual ensemble conformational change. Structural changes upon ligand binding are monitored by combination of small angle x-ray scattering (SAXS) and NMR spectroscopy. Detailed structure characterization of GlnBP contributes to a better understanding of ligand binding and provides the structural basis for biosensor design.

DOI10.1371/journal.pone.0263102
URLView the original
Indexed BySCIE
Language英語English
WOS Research AreaScience & Technology - Other Topics
WOS SubjectMultidisciplinary Sciences
WOS IDWOS:000795468200031
Scopus ID2-s2.0-85128604662
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Cited Times [WOS]:0   [WOS Record]     [Related Records in WOS]
Document TypeJournal article
CollectionUniversity of Macau
Corresponding AuthorYang, Chengming; Yu, Dongmei
Affiliation1.Center of Precision Medicine and Healthcare, Tsinghua-Berkeley Shenzhen Institute, Shenzhen, Guangdong Province, China
2.X-ray Science Division, Argonne National Laboratory, Argonne, United States
3.Institute of Chinese medical sciences, University of Macau, Macao
4.Shenzhen Aier Eye Hospital, Guangdong Province, Futian District, China
5.University of Science and Technology Hospital, Shenzhen, Guangdong Province, China
6.Food Inspection & Quarantine Center, Shenzhen Custom, Shenzhen, Guangdong, China
7.Shenzhen Maternity and Child Healthcare Hospital, Affiliated to Southern Medical University, Shenzhen, Guangdong, China
8.School of Mechanical, Electrical & Information Engineering, Shandong University, Weihai, Shandong Province, China
Recommended Citation
GB/T 7714
Chen, Qun,Li, Fang,Zuo, Xiaobing,et al. Reversible domain closure modulates GlnBP ligand binding affinity[J]. PLoS ONE,2022,17(4 April).
APA Chen, Qun,Li, Fang,Zuo, Xiaobing,Chen, Jin,Qin, Peiwu,Wang, Chuhui,Xu, Jin,Yang, Danyu,Xing, Baogang,Liu, Ying,Jia, Peng,Li, Linling,Yang, Chengming,&Yu, Dongmei.(2022).Reversible domain closure modulates GlnBP ligand binding affinity.PLoS ONE,17(4 April).
MLA Chen, Qun,et al."Reversible domain closure modulates GlnBP ligand binding affinity".PLoS ONE 17.4 April(2022).
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