5YHF
Crystal structure of SecDF in Super-membrane-facing form
Summary for 5YHF
| Entry DOI | 10.2210/pdb5yhf/pdb |
| Descriptor | Protein translocase subunit SecDF, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, DI(HYDROXYETHYL)ETHER, ... (4 entities in total) |
| Functional Keywords | membrane protein, beta barrel, transport protein, motor protein |
| Biological source | Thermus thermophilus |
| Cellular location | Cell inner membrane ; Multi- pass membrane protein : Q5SKE6 |
| Total number of polymer chains | 1 |
| Total formula weight | 82478.58 |
| Authors | Tanaka, Y.,Tsukazaki, T.,Yoshikaie, K.,Furukawa, A. (deposition date: 2017-09-28, release date: 2018-02-14, Last modification date: 2023-11-22) |
| Primary citation | Furukawa, A.,Nakayama, S.,Yoshikaie, K.,Tanaka, Y.,Tsukazaki, T. Remote Coupled Drastic beta-Barrel to beta-Sheet Transition of the Protein Translocation Motor. Structure, 26:485-489.e2, 2018 Cited by PubMed Abstract: The membrane protein SecDF, belonging to the RND superfamily, enhances protein translocation at the extracytoplasmic side using a proton gradient. Here, we report the crystal structure of SecDF in a form we named Super-membrane-facing (Super F) form, demonstrating a β-barrel architecture instead of the previously reported β-sheet structure. Through this structural insight and supporting results of an in vivo crosslinking experiment, we propose a remote coupling model in which a structural change of the transmembrane region drives a functional, extracytoplasmic conformational transition. PubMed: 29398525DOI: 10.1016/j.str.2018.01.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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