期刊
JOURNAL OF CHEMICAL INFORMATION AND MODELING
卷 61, 期 2, 页码 891-900出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jcim.0c01119
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资金
- Ministry of Science and Technology of the People's Republic of China [2016YFA0501702]
- National Natural Science Foundation of China [21773038, 22073018]
- Shanghai Municipal Science and Technology Major Project [2018SHZDZX01]
- Zhangjiang Lab Foundation [Y93Z011D01]
The D-glucose/D-galactose-binding protein (GGBP) from Escherichia coli is a substrate-binding protein (SBP) associated with sugar transport and chemotaxis. It is also a calcium-binding protein, and the study found that calcium binding can stabilize the open conformation of GGBP, playing an active regulatory role in tuning the conformational distribution of the protein.
The D-glucose/D-galactose-binding protein (GGBP) from Escherichia coli is a substrate-binding protein (SBP) associated with sugar transport and chemotaxis. It is also a calcium-binding protein, which makes it unique in the SBP family. However, the functional importance of Ca2+ binding is not fully understood. Here, the calcium-dependent properties of GGBP were explored by all-atom molecular dynamics simulations and Markov state model (MSM) analysis as well as single-molecule Forster resonance energy transfer (smFRET) measurements. In agreement with previous experimental studies, we observed the structure stabilization effect of Ca2+ binding on the C-terminal domain of GGBP, especially theCa(2+)-binding site. Interestingly, the MSMs of calcium-depleted GGBP and calcium-bound GGBP (GGBP/Ca2+) demonstrate that Ca2+ greatly stabilizes the open conformation, and smFRET measurements confirmed this result. Further analysis reveals that Ca2+ binding disturbs the local hydrogen bonding interactions and the conformational dynamics of the hinge region, thereby weakening the long-range interdomain correlations to favor the open conformation. These results suggest an active regulatory role of Ca2+ binding in GGBP, which finely tunes the conformational distribution. The work sheds new light on the study of calcium-binding proteins in prokaryotes.
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