Title: | Structure of bacterial cellulose synthase subunit D octamer with four inner passageways |
Authors: | Hu, Song-Qing Browse this author |
Gao, Yong-Gui Browse this author |
Tajima, Kenji Browse this author |
Sunagawa, Naoki Browse this author |
Zhou, Yong Browse this author |
Kawano, Shin Browse this author |
Fujiwara, Takaaki Browse this author |
Yoda, Takanori Browse this author |
Shimura, Daisuke Browse this author |
Satoh, Yasuharu Browse this author |
Munekata, Masanobu Browse this author |
Tanaka, Isao Browse this author |
Yao, Min Browse this author |
Keywords: | crystal structure |
cellulose biosynthesis |
Issue Date: | 19-Oct-2010 |
Publisher: | National Academy of Sciences |
Journal Title: | Proceedings of the National Academy of Sciences of the United States of America |
Volume: | 107 |
Issue: | 42 |
Start Page: | 17957 |
End Page: | 17961 |
Publisher DOI: | 10.1073/pnas.1000601107 |
Abstract: | The cellulose synthesizing terminal complex consisting of subunits A, B, C, and D in Acetobacter xylinum spans the outer and inner cell membranes to synthesize and extrude glucan chains, which are assembled into sub-elementary fibrils and further into a ribbon. We determined the structures of subunit D (AxCeSD/AxBcsD) with both N- and C-terminal His6-tag, and in complex with cellopentaose. The structure of AxCeSD shows an exquisite cylinder shape (height: ∼65Å, outer diameter: ∼90Å, and inner diameter: ∼25Å) with a right-hand twisted dimer interface on the cylinder-wall, formed by octamer as a functional unit. All N-termini of the octamer are positioned inside the AxCeSD cylinder and create four passageways. The location of cellopentaoses in the complex structure suggests that four glucan chains are extruded individually through their own passageway along the dimer interface in a twisted manner. The complex structure also shows that the N-terminal loop, especially residue Lys6, seems to be important for cellulose production, as confirmed by in vivo assay using mutant cells with axcesD gene disruption and N-terminus truncation. Taking all results together, a model of the bacterial terminal complex is discussed. |
Type: | article (author version) |
URI: | http://hdl.handle.net/2115/45250 |
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)
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