6RAD

Salmonella ATPase InvC with ADP

6RAD の概要

• エントリーDOI: 10.2210/pdb6rad/pdb
• 分子名称: Secretory apparatus ATP synthase (Associated with virulence), ADENOSINE-5'-DIPHOSPHATE, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (6 entities in total)
• 機能のキーワード: bacterial pathogenesis, salmonella enterica, type iii secretion system (t3ss), atpase, crystallography., hydrolase
• 由来する生物種: Salmonella typhimurium (strain SL1344)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41441.76

構造登録者

Bernal, I.,Roemermann, J.,Flacht, L.,Lunelli, M.,Uetrecht, C.,Kolbe, M. (登録日: 2019-04-05, 公開日: 2019-08-21, 最終更新日: 2024-05-15)

主引用文献

Bernal, I.,Romermann, J.,Flacht, L.,Lunelli, M.,Uetrecht, C.,Kolbe, M.
Structural analysis of ligand-bound states of the Salmonella type III secretion system ATPase InvC.
Protein Sci., 28:1888-1901, 2019

PubMed Abstract: Translocation of virulence effector proteins through the type III secretion system (T3SS) is essential for the virulence of many medically relevant Gram-negative bacteria. The T3SS ATPases are conserved components that specifically recognize chaperone-effector complexes and energize effector secretion through the system. It is thought that functional T3SS ATPases assemble into a cylindrical structure maintained by their N-terminal domains. Using size-exclusion chromatography coupled to multi-angle light scattering and native mass spectrometry, we show that in the absence of the N-terminal oligomerization domain the Salmonella T3SS ATPase InvC can form monomers and dimers in solution. We also present for the first time a 2.05 å resolution crystal structure of InvC lacking the oligomerization domain (InvCΔ79) and map the amino acids suggested for ATPase intersubunit interaction, binding to other T3SS proteins and chaperone-effector recognition. Furthermore, we validate the InvC ATP-binding site by co-crystallization of InvCΔ79 with ATPγS (2.65 å) and ADP (2.80 å). Upon ATP-analogue recognition, these structures reveal remodeling of the ATP-binding site and conformational changes of two loops located outside of the catalytic site. Both loops face the central pore of the predicted InvC cylinder and are essential for the function of the T3SS ATPase. Our results present a fine functional and structural correlation of InvC and provide further details of the homo-oligomerization process and ATP-dependent conformational changes underlying the T3SS ATPase activity.

PubMed: 31393998
DOI: 10.1002/pro.3704

実験手法

X-RAY DIFFRACTION (2.796 Å)