4X5M
Crystal structure of SemiSWEET in the inward-open conformation
Summary for 4X5M
| Entry DOI | 10.2210/pdb4x5m/pdb |
| Related | 4X5N |
| Descriptor | Uncharacterized protein, OLEIC ACID, (2S)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (6 entities in total) |
| Functional Keywords | sweet, pqlc, membrane protein, sugar transporter, transport protein |
| Biological source | Escherichia coli UMEA 3162-1 |
| Total number of polymer chains | 3 |
| Total formula weight | 38425.27 |
| Authors | Lee, Y.,Nishizawa, T.,Yamashita, K.,Ishitani, R.,Nureki, O. (deposition date: 2014-12-05, release date: 2015-01-21, Last modification date: 2024-03-20) |
| Primary citation | Lee, Y.,Nishizawa, T.,Yamashita, K.,Ishitani, R.,Nureki, O. Structural basis for the facilitative diffusion mechanism by SemiSWEET transporter Nat Commun, 6:6112-6112, 2015 Cited by PubMed Abstract: SWEET family proteins mediate sugar transport across biological membranes and play crucial roles in plants and animals. The SWEETs and their bacterial homologues, the SemiSWEETs, are related to the PQ-loop family, which is characterized by highly conserved proline and glutamine residues (PQ-loop motif). Although the structures of the bacterial SemiSWEETs were recently reported, the conformational transition and the significance of the conserved motif in the transport cycle have remained elusive. Here we report crystal structures of SemiSWEET from Escherichia coli, in the both inward-open and outward-open states. A structural comparison revealed that SemiSWEET undergoes an intramolecular conformational change in each protomer. The conserved PQ-loop motif serves as a molecular hinge that enables the 'binder clip-like' motion of SemiSWEET. The present work provides the framework for understanding the overall transport cycles of SWEET and PQ-loop family proteins. PubMed: 25598322DOI: 10.1038/ncomms7112 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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