Structural highlights
Function
[SECDF_THET8] Conducts protons, which can be regulated by a proton gradient or by binding of an unfolded protein. Proton conduction requires the large periplasmic domain of the SecD.[HAMAP-Rule:MF_01463_B] Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.[HAMAP-Rule:MF_01463_B]
Publication Abstract from PubMed
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 beta-barrel architecture instead of the previously reported beta-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.
Remote Coupled Drastic beta-Barrel to beta-Sheet Transition of the Protein Translocation Motor.,Furukawa A, Nakayama S, Yoshikaie K, Tanaka Y, Tsukazaki T Structure. 2018 Jan 26. pii: S0969-2126(18)30002-9. doi:, 10.1016/j.str.2018.01.002. PMID:29398525[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. 2018 Jan 26. pii: S0969-2126(18)30002-9. doi:, 10.1016/j.str.2018.01.002. PMID:29398525 doi:http://dx.doi.org/10.1016/j.str.2018.01.002
