Maltose-binding protein effectively stabilizes the partially closed conformation of the ATP-binding cassette transporter MalFGK2

Jingwei Weng; Shuo Gu; Xin Gao; Xuhui Huang; Wenning Wang

doi:10.1039/c6cp07943a

Maltose-binding protein effectively stabilizes the partially closed conformation of the ATP-binding cassette transporter MalFGK2

Jingwei Weng, Shuo Gu, Xin Gao, Xuhui Huang, Wenning Wang

Research output: Contribution to journal › Article › peer-review

8 Scopus citations

Abstract

Maltose transporter MalFGK2 is a type-I importer in the ATP-binding cassette (ABC) transporter superfamily. Upon the binding of its periplasmic binding protein, MalE, the ATPase activity of MalFGK2 can be greatly enhanced. Crystal structures of the MalFGK2-MalE-maltose complex in a so-called

Original language	English (US)
Pages (from-to)	9366-9373
Number of pages	8
Journal	Phys. Chem. Chem. Phys.
Volume	19
Issue number	14
DOIs	https://doi.org/10.1039/c6cp07943a
State	Published - 2017

Bibliographical note

KAUST Repository Item: Exported on 2020-10-01
Acknowledgements: This work was supported by National Major Basic Research Program of China (2016YFA0501702), National Science Foundation of China (21473034, 21403036), and Specialized Research Fund for the Doctoral Program of Higher Education (20130071140004). X. H. acknowledges the Hong Kong Research Grants Council (M-HKUST601/13, 609813, 16302214, 16304215, and HKUST C6009-15G). X. G. thanks the support by funding from King Abdullah University of Science and Technology (KAUST). This research made use of the resources of the computer clusters at KAUST and the super computer center at Fudan University.

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title = "Maltose-binding protein effectively stabilizes the partially closed conformation of the ATP-binding cassette transporter MalFGK2",

abstract = "Maltose transporter MalFGK2 is a type-I importer in the ATP-binding cassette (ABC) transporter superfamily. Upon the binding of its periplasmic binding protein, MalE, the ATPase activity of MalFGK2 can be greatly enhanced. Crystal structures of the MalFGK2-MalE-maltose complex in a so-called",

author = "Jingwei Weng and Shuo Gu and Xin Gao and Xuhui Huang and Wenning Wang",

note = "KAUST Repository Item: Exported on 2020-10-01 Acknowledgements: This work was supported by National Major Basic Research Program of China (2016YFA0501702), National Science Foundation of China (21473034, 21403036), and Specialized Research Fund for the Doctoral Program of Higher Education (20130071140004). X. H. acknowledges the Hong Kong Research Grants Council (M-HKUST601/13, 609813, 16302214, 16304215, and HKUST C6009-15G). X. G. thanks the support by funding from King Abdullah University of Science and Technology (KAUST). This research made use of the resources of the computer clusters at KAUST and the super computer center at Fudan University.",

year = "2017",

doi = "10.1039/c6cp07943a",

language = "English (US)",

volume = "19",

pages = "9366--9373",

journal = "Phys. Chem. Chem. Phys.",

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publisher = "Royal Society of Chemistry",

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T1 - Maltose-binding protein effectively stabilizes the partially closed conformation of the ATP-binding cassette transporter MalFGK2

AU - Weng, Jingwei

AU - Gu, Shuo

AU - Gao, Xin

AU - Huang, Xuhui

AU - Wang, Wenning

N1 - KAUST Repository Item: Exported on 2020-10-01 Acknowledgements: This work was supported by National Major Basic Research Program of China (2016YFA0501702), National Science Foundation of China (21473034, 21403036), and Specialized Research Fund for the Doctoral Program of Higher Education (20130071140004). X. H. acknowledges the Hong Kong Research Grants Council (M-HKUST601/13, 609813, 16302214, 16304215, and HKUST C6009-15G). X. G. thanks the support by funding from King Abdullah University of Science and Technology (KAUST). This research made use of the resources of the computer clusters at KAUST and the super computer center at Fudan University.

PY - 2017

Y1 - 2017

N2 - Maltose transporter MalFGK2 is a type-I importer in the ATP-binding cassette (ABC) transporter superfamily. Upon the binding of its periplasmic binding protein, MalE, the ATPase activity of MalFGK2 can be greatly enhanced. Crystal structures of the MalFGK2-MalE-maltose complex in a so-called

AB - Maltose transporter MalFGK2 is a type-I importer in the ATP-binding cassette (ABC) transporter superfamily. Upon the binding of its periplasmic binding protein, MalE, the ATPase activity of MalFGK2 can be greatly enhanced. Crystal structures of the MalFGK2-MalE-maltose complex in a so-called

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JO - Phys. Chem. Chem. Phys.

JF - Phys. Chem. Chem. Phys.

IS - 14

ER -

Maltose-binding protein effectively stabilizes the partially closed conformation of the ATP-binding cassette transporter MalFGK2

Abstract

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