|
Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Life Science / Faculty of Advanced Life Science >
Peer-reviewed Journal Articles, etc >
Crystal structure of the flexible tandem repeat domain of bacterial cellulose synthesis subunit C
This item is licensed under:Creative Commons Attribution 4.0 International
| Title: | Crystal structure of the flexible tandem repeat domain of bacterial cellulose synthesis subunit C |
| Authors: | Nojima, Shingo Browse this author | | Fujishima, Ayumi Browse this author | | Kato, Koji Browse this author | | Ohuchi, Kayoko Browse this author | | Shimizu, Nobutaka Browse this author | | Yonezawa, Kento Browse this author | | Tajima, Kenji Browse this author | | Yao, Min Browse this author →KAKEN DB |
| Issue Date: | 12-Oct-2017 |
| Publisher: | Nature Publishing Group |
| Journal Title: | Scientific reports |
| Volume: | 7 |
| Start Page: | 13018 |
| Publisher DOI: | 10.1038/s41598-017-12530-0 |
| Abstract: | Bacterial cellulose (BC) is synthesized and exported through the cell membrane via a large protein complex (terminal complex) that consists of three or four subunits. BcsC is a little-studied subunit considered to export BC to the extracellular matrix. It is predicted to have two domains: a tetratrico peptide repeat (TPR) domain and a beta-barrelled outer membrane domain. Here we report the crystal structure of the N-terminal part of BcsC-TPR domain (Asp24-Arg272) derived from Enterobacter CJF-002. Unlike most TPR-containing proteins which have continuous TPR motifs, this structure has an extra a-helix between two clusters of TPR motifs. Five independent molecules in the crystal had three different conformations that varied at the hinge of the inserted a-helix. Such structural feature indicates that the inserted a-helix confers flexibility to the chain and changes the direction of the TPR super-helix, which was also suggested by structural analysis of BcsC-TPR (Asp24-Leu664) in solution by size exclusion chromatography-small-angle X-ray scattering. The flexibility at the a-helical hinge may play important role for exporting glucan chains. |
| Rights: | http://creativecommons.org/licenses/by/4.0/ |
| Type: | article |
| URI: | http://hdl.handle.net/2115/67750 |
| Appears in Collections: | 生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
|
Submitter: 姚 閔
|
