4BZA

Crystal structure of TamA POTRA domains 1-3 from E. coli

4BZA の概要

• エントリーDOI: 10.2210/pdb4bza/pdb
• 関連するPDBエントリー: 4C00
• 分子名称: TRANSLOCATION AND ASSEMBLY MODULE TAMA, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: transport protein, polypeptide transport-associated, autotransporter biogenesis, outer membrane protein
• 由来する生物種: ESCHERICHIA COLI
• 細胞内の位置: Cell outer membrane: P0ADE4
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29535.30

構造登録者

Jakob, R.P.,Gruss, F.,Zaehringer, F.,Burmann, B.M.,Hiller, S.,Maier, T. (登録日: 2013-07-24, 公開日: 2013-09-25, 最終更新日: 2024-05-08)

主引用文献

Gruss, F.,Zaehringer, F.,Jakob, R.P.,Burmann, B.M.,Hiller, S.,Maier, T.
The Structural Basis of Autotransporter Translocation by Tama
Nat.Struct.Mol.Biol., 20:1318-, 2013

PubMed Abstract: TamA is an Escherichia coli Omp85 protein involved in autotransporter biogenesis. It comprises a 16-stranded transmembrane β-barrel and three POTRA domains. The 2.3-Å crystal structure reveals that the TamA barrel is closed at the extracellular face by a conserved lid loop. The C-terminal β-strand of the barrel forms an unusual inward kink, which weakens the lateral barrel wall and creates a gate for substrate access to the lipid bilayer.

PubMed: 24056943
DOI: 10.1038/NSMB.2689

実験手法

X-RAY DIFFRACTION (1.839 Å)