3WDO
Structure of E. coli YajR transporter
3WDO の概要
| エントリーDOI | 10.2210/pdb3wdo/pdb |
| 分子名称 | MFS Transporter (1 entity in total) |
| 機能のキーワード | motif a, membrane potential, protonation, transport protein |
| 由来する生物種 | Escherichia coli |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 48678.45 |
| 構造登録者 | |
| 主引用文献 | Jiang, D.,Zhao, Y.,Wang, X.,Fan, J.,Heng, J.,Liu, X.,Feng, W.,Kang, X.,Huang, B.,Liu, J.,Zhang, X.C. Structure of the YajR transporter suggests a transport mechanism based on the conserved motif A Proc.Natl.Acad.Sci.USA, 110:14664-14669, 2013 Cited by PubMed Abstract: The major facilitator superfamily (MFS) is the largest family of secondary active transporters and is present in all life kingdoms. Detailed structural basis of the substrate transport and energy-coupling mechanisms of these proteins remain to be elucidated. YajR is a putative proton-driven MFS transporter found in many Gram-negative bacteria. Here we report the crystal structure of Escherichia coli YajR at 3.15 Å resolution in an outward-facing conformation. In addition to having the 12 canonical transmembrane helices, the YajR structure includes a unique 65-residue C-terminal domain which is independently stable. The structure is unique in illustrating the functional role of "sequence motif A." This highly conserved element is seen to stabilize the outward conformation of YajR and suggests a general mechanism for the conformational change between the inward and outward states of the MFS transporters. PubMed: 23950222DOI: 10.1073/pnas.1308127110 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.15 Å) |
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