4HZU
Structure of a bacterial energy-coupling factor transporter
Summary for 4HZU
| Entry DOI | 10.2210/pdb4hzu/pdb |
| Descriptor | Energy-coupling factor transporter ATP-binding protein EcfA 1, Energy-coupling factor transporter ATP-binding protein EcfA 2, Energy-coupling factor transporter transmembrane protein EcfT, ... (4 entities in total) |
| Functional Keywords | membrane protein, ecf, transporter, hydrolase, transport protein |
| Biological source | Lactobacillus brevis More |
| Cellular location | Cell membrane; Peripheral membrane protein (By similarity): Q03PY6 Q03PY5 Cell membrane; Multi-pass membrane protein (Potential): Q03PY7 |
| Total number of polymer chains | 4 |
| Total formula weight | 110457.11 |
| Authors | Wang, T.L.,Fu, G.B.,Pan, X.J.,Shi, Y.G. (deposition date: 2012-11-15, release date: 2013-04-17, Last modification date: 2024-02-28) |
| Primary citation | Wang, T.,Fu, G.,Pan, X.,Wu, J.,Gong, X.,Wang, J.,Shi, Y. Structure of a bacterial energy-coupling factor transporter. Nature, 497:272-276, 2013 Cited by PubMed Abstract: The energy-coupling factor (ECF) transporters constitute a novel family of conserved membrane transporters in prokaryotes that have a similar domain organization to the ATP-binding cassette transporters. Each ECF transporter comprises a pair of cytosolic ATPases (the A and A' components, or EcfA and EcfA'), a membrane-embedded substrate-binding protein (the S component, or EcfS) and a transmembrane energy-coupling component (the T component, or EcfT) that links the EcfA-EcfA' subcomplex to EcfS. The structure and transport mechanism of the quaternary ECF transporter remain largely unknown. Here we report the crystal structure of a nucleotide-free ECF transporter from Lactobacillus brevis at a resolution of 3.5 Å. The T component has a horseshoe-shaped open architecture, with five α-helices as transmembrane segments and two cytoplasmic α-helices as coupling modules connecting to the A and A' components. Strikingly, the S component, thought to be specific for hydroxymethyl pyrimidine, lies horizontally along the lipid membrane and is bound exclusively by the five transmembrane segments and the two cytoplasmic helices of the T component. These structural features suggest a plausible working model for the transport cycle of the ECF transporters. PubMed: 23584587DOI: 10.1038/nature12045 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.53 Å) |
Structure validation
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