The bacterial dicarboxylate transporter VcINDY uses a two-domain elevator-type mechanism

被引:0
作者
Christopher Mulligan
Cristina Fenollar-Ferrer
Gabriel A Fitzgerald
Ariela Vergara-Jaque
Desirée Kaufmann
Yan Li
Lucy R Forrest
Joseph A Mindell
机构
[1] Membrane Transport Biophysics Section,
[2] National Institute of Neurological Disorders and Stroke,undefined
[3] National Institutes of Health,undefined
[4] Computational Structural Biology Unit,undefined
[5] National Institute of Neurological Disorders and Stroke,undefined
[6] National Institutes of Health,undefined
[7] Max Planck Institute of Biophysics,undefined
[8] Protein/Peptide Sequencing Facility,undefined
[9] Porter Neuroscience Research Center,undefined
[10] National Institute of Neurological Disorders and Stroke,undefined
[11] National Institutes of Health,undefined
[12] Present addresses: Department of Physiology,undefined
[13] Weill Cornell Medical College,undefined
[14] New York,undefined
[15] New York,undefined
[16] USA (G.A.F.),undefined
[17] and Institute of Molecular Biology,undefined
[18] Mainz,undefined
[19] Germany (D.K.).,undefined
来源
Nature Structural & Molecular Biology | 2016年 / 23卷
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学科分类号
摘要
‘Repeat swap’ modeling of the outward-facing conformation and biochemical analyses show that the bacterial VcINDY symporter uses an elevator-type mechanism for substrate transport across the cell membrane.
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页码:256 / 263
页数:7
相关论文
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