3WDO
Structure of E. coli YajR transporter
Summary for 3WDO
| Entry DOI | 10.2210/pdb3wdo/pdb |
| Descriptor | MFS Transporter (1 entity in total) |
| Functional Keywords | motif a, membrane potential, protonation, transport protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 48678.45 |
| Authors | Jiang, D. (deposition date: 2013-06-19, release date: 2013-08-07, Last modification date: 2024-03-20) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.15 Å) |
Structure validation
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