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-Structure paper
タイトル | Membrane translocation process revealed by in situ structures of type II secretion system secretins. |
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ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 4025, Year 2023 |
掲載日 | 2023年7月7日 |
![]() | Zhili Yu / Yaoming Wu / Muyuan Chen / Tong Huo / Wei Zheng / Steven J Ludtke / Xiaodong Shi / Zhao Wang / ![]() ![]() |
PubMed 要旨 | The GspD secretin is the outer membrane channel of the bacterial type II secretion system (T2SS) which secrets diverse toxins that cause severe diseases such as diarrhea and cholera. GspD needs to ...The GspD secretin is the outer membrane channel of the bacterial type II secretion system (T2SS) which secrets diverse toxins that cause severe diseases such as diarrhea and cholera. GspD needs to translocate from the inner to the outer membrane to exert its function, and this process is an essential step for T2SS to assemble. Here, we investigate two types of secretins discovered so far in Escherichia coli, GspD, and GspD. By electron cryotomography subtomogram averaging, we determine in situ structures of key intermediate states of GspD and GspD in the translocation process, with resolution ranging from 9 Å to 19 Å. In our results, GspD and GspD present entirely different membrane interaction patterns and ways of transitioning the peptidoglycan layer. From this, we hypothesize two distinct models for the membrane translocation of GspD and GspD, providing a comprehensive perspective on the inner to outer membrane biogenesis of T2SS secretins. |
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手法 | EM (サブトモグラム平均) |
解像度 | 9.0 - 19.0 Å |
構造データ | ![]() EMDB-29696: In situ structure of GspD-beta-GspS complex on the bacterial outer membrane ![]() EMDB-29697: In situ structure of GspD-beta-GspS complex on the bacterial outer membrane when GspD-beta is overexpressed solely ![]() EMDB-29698: In situ structure of GspD-beta on the bacterial inner membrane ![]() EMDB-29702: In situ structure of GspD-alpha on the bacterial inner membrane ![]() EMDB-29703: In situ structure of GspD-alpha on the bacterial outer membrane |
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