Structural remodelling of the carbon–phosphorus lyase machinery by a dual ABC ATPase
Here, authors analyse the structural organisation of the large carbon-phosphorus lyase enzyme from bacteria using electron microscopy and discover that it contains two ATP-binding cassette dimers of PhnK and PhnL and opens upon ATP hydrolysis.
Main Authors: | Søren K. Amstrup, Sui Ching Ong, Nicholas Sofos, Jesper L. Karlsen, Ragnhild B. Skjerning, Thomas Boesen, Jan J. Enghild, Bjarne Hove-Jensen, Ditlev E. Brodersen |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Portfolio
2023-02-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-023-36604-y |
Similar Items
-
Studies of the ATPase activity of the ABC protein SUR1.
by: De Wet, H, et al.
Published: (2007) -
Coupled ATPase-adenylate kinase activity in ABC transporters
by: Hundeep Kaur, et al.
Published: (2016-12-01) -
Clamp loader ATPases and the evolution of DNA replication machinery
by: Kelch Brian A, et al.
Published: (2012-04-01) -
An asymmetric post-hydrolysis state of the ABC transporter ATPase dimer.
by: Anthony M George, et al.
Published: (2013-01-01) -
A Highly Active Chondroitin Sulfate Lyase ABC for Enzymatic Depolymerization of Chondroitin Sulfate
by: Xiao-Man Fan, et al.
Published: (2022-04-01)