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3A8E

The structure of AxCesD octamer complexed with cellopentaose

3A8E の概要
エントリーDOI10.2210/pdb3a8e/pdb
関連するPDBエントリー2Z9E 2Z9F
関連するBIRD辞書のPRD_IDPRD_900016
分子名称Cellulose synthase operon protein D, beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose (3 entities in total)
機能のキーワードcomplex, octamer, tetramer of dimers, molecule ring, cellulose biosynthesis, bcsd, tc, biosynthetic protein
由来する生物種Acetobacter xylinus (Gluconacetobacter xylinus)
タンパク質・核酸の鎖数4
化学式量合計75357.02
構造登録者
Hu, S.Q.,Tajima, K.,Zhou, Y.,Yao, M.,Tanaka, I. (登録日: 2009-10-05, 公開日: 2010-09-22, 最終更新日: 2023-11-01)
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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3 Å)
構造検証レポート
Validation report summary of 3a8e
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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