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Structure of bacterial cellulose synthase subunit D octamer with four inner passageways

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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)

Submitter: 姚 閔

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