3O7P
Crystal structure of the E.coli Fucose:proton symporter, FucP (N162A)
Summary for 3O7P
| Entry DOI | 10.2210/pdb3o7p/pdb |
| Related | 3O7Q |
| Descriptor | L-fucose-proton symporter, nonyl beta-D-glucopyranoside (2 entities in total) |
| Functional Keywords | l-fucose, symporter, multi-pass membrane protein, transporter, transport protein |
| Biological source | Escherichia coli |
| Cellular location | Cell inner membrane; Multi-pass membrane protein: P11551 |
| Total number of polymer chains | 1 |
| Total formula weight | 47837.94 |
| Authors | Dang, S.Y.,Sun, L.F.,Wang, J.,Yan, N. (deposition date: 2010-07-30, release date: 2010-09-15, Last modification date: 2023-11-01) |
| Primary citation | Dang, S.Y.,Sun, L.F.,Huang, Y.,Lu, F.,Liu, Y.,Gong, H.,Wang, J.,Yan, N. Structure of a fucose transporter in an outward-open conformation Nature, 467:734-738, 2010 Cited by PubMed Abstract: The major facilitator superfamily (MFS) transporters are an ancient and widespread family of secondary active transporters. In Escherichia coli, the uptake of l-fucose, a source of carbon for microorganisms, is mediated by an MFS proton symporter, FucP. Despite intensive study of the MFS transporters, atomic structure information is only available on three proteins and the outward-open conformation has yet to be captured. Here we report the crystal structure of FucP at 3.1 Å resolution, which shows that it contains an outward-open, amphipathic cavity. The similarly folded amino and carboxyl domains of FucP have contrasting surface features along the transport path, with negative electrostatic potential on the N domain and hydrophobic surface on the C domain. FucP only contains two acidic residues along the transport path, Asp 46 and Glu 135, which can undergo cycles of protonation and deprotonation. Their essential role in active transport is supported by both in vivo and in vitro experiments. Structure-based biochemical analyses provide insights into energy coupling, substrate recognition and the transport mechanism of FucP. PubMed: 20877283DOI: 10.1038/nature09406 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.196 Å) |
Structure validation
Download full validation report
