3AJ1

The structure of AxCeSD octamer (N-terminal HIS-tag) from Acetobacter xylinum

「2Z9E」から置き換えられました

3AJ1 の概要

• エントリーDOI: 10.2210/pdb3aj1/pdb
• 関連するPDBエントリー: 2Z9E 3AJ2
• 分子名称: Cellulose synthase operon protein D (2 entities in total)
• 機能のキーワード: alpha and beta fold, octamer, tetramer of dimers, molecule ring, cellulose biosynthesis, biosynthetic protein, structural genomics, nppsfa, national project on protein structural and functional analyses
• 由来する生物種: ACETOBACTER XYLINUS (Gluconacetobacter xylinus)
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 151909.25

構造登録者

Hu, S.Q.,Tajima, K.,Zhou, Y.,Tanaka, I.,Yao, M. (登録日: 2010-05-20, 公開日: 2010-10-06, 最終更新日: 2024-10-16)

主引用文献

Hu, S.Q.,Gao, Y.G.,Tajima, K.,Sunagawa, N.,Zhou, Y.,Kawano, S.,Fujiwara, T.,Yoda, T.,Shimura, D.,Satoh, Y.,Munekata, M.,Tanaka, I.,Yao, M.
Structure of bacterial cellulose synthase subunit D octamer with four inner passageways
Proc.Natl.Acad.Sci.USA, 107:17957-17961, 2010

PubMed 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 subelementary fibrils and further into a ribbon. We determined the structures of subunit D (AxCeSD/AxBcsD) with both N- and C-terminal His(6) tags, and in complex with cellopentaose. The structure of AxCeSD shows an exquisite cylinder shape (height: ∼65 Å, outer diameter: ∼90 Å, and inner diameter: ∼25 Å) 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.

PubMed: 20921370
DOI: 10.1073/pnas.1000601107

実験手法

X-RAY DIFFRACTION (2.5 Å)