3B0Z

Crystal structure of cytoplasmic domain of FlhB from Salmonella typhimurium

3B0Z の概要

• エントリーDOI: 10.2210/pdb3b0z/pdb
• 関連するPDBエントリー: 3b1s
• 分子名称: Flagellar biosynthetic protein flhB, ZINC ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: flagella, type iii secretion system, protein transport, membrane protein
• 由来する生物種: Salmonella enterica subsp. enterica serovar Typhimurium; 詳細
• 細胞内の位置: Cell inner membrane ; Multi- pass membrane protein : P40727 P40727
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19005.47

構造登録者

Meshcheryakov, V.A.,Samatey, F.A. (登録日: 2011-06-17, 公開日: 2012-06-20, 最終更新日: 2024-03-13)

主引用文献

Meshcheryakov, V.A.,Kitao, A.,Matsunami, H.,Samatey, F.A.
Inhibition of a type III secretion system by the deletion of a short loop in one of its membrane proteins
Acta Crystallogr.,Sect.D, 69:812-820, 2013

PubMed Abstract: The membrane protein FlhB is a highly conserved component of the flagellar secretion system. It is composed of an N-terminal transmembrane domain and a C-terminal cytoplasmic domain (FlhBC). Here, the crystal structures of FlhBC from Salmonella typhimurium and Aquifex aeolicus are described at 2.45 and 2.55 Å resolution, respectively. These flagellar FlhBC structures are similar to those of paralogues from the needle type III secretion system, with the major difference being in a linker that connects the transmembrane and cytoplasmic domains of FlhB. It was found that deletion of a short flexible loop in a globular part of Salmonella FlhBC leads to complete inhibition of secretion by the flagellar secretion system. Molecular-dynamics calculations demonstrate that the linker region is the most flexible part of FlhBC and that the deletion of the loop reduces this flexibility. These results are in good agreement with previous studies showing the importance of the linker in the function of FlhB and provide new insight into the relationship between the different parts of the FlhBC molecule.

PubMed: 23633590
DOI: 10.1107/S0907444913002102

実験手法

X-RAY DIFFRACTION (2.45 Å)