- Formation of a distinctive complex between the inducible bacterial lysine decarboxylase and a novel AAA+ ATPaseJamie Snider
Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada
J Biol Chem 281:1532-46. 2006..AAA+ chaperones in Escherichia coli, we report the characterization of a representative member of the MoxR family, YieN, which we have renamed RavA (regulatory ATPase variant A)...
- MoxR AAA+ ATPases: a novel family of molecular chaperones?Jamie Snider
Department of Biochemistry, University of Toronto, 1 King s College Circle, Medical Sciences Building, Toronto, Ont, Canada M5S 1A8
J Struct Biol 156:200-9. 2006..reveals that the MoxR family can be divided into at least seven subfamilies, including MoxR Proper (MRP), TM0930, RavA, CGN, APE2220, PA2707, and YehL...
- Structure of RavA MoxR AAA+ protein reveals the design principles of a molecular cage modulating the inducible lysine decarboxylase activityMajida El Bakkouri
Department of Biochemistry, University of Toronto, Toronto, ON, Canada M5S 1A8
Proc Natl Acad Sci U S A 107:22499-504. 2010..We recently found that the Escherichia coli MoxR protein, RavA (Regulatory ATPase variant A), tightly interacts with the inducible lysine decarboxylase, LdcI/CadA, to form a ..
- The MoxR ATPase RavA and its cofactor ViaA interact with the NADH:ubiquinone oxidoreductase I in Escherichia coliKeith S Wong
Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada
PLoS ONE 9:e85529. 2014..In Escherichia coli, the MoxR ATPase RavA and its putative cofactor ViaA are found to exist in early stationary-phase cells at 37 °C at low levels of about ..
- Assembly principles of a unique cage formed by hexameric and decameric E. coli proteinsHelene Malet
European Molecular Biology Laboratory, Grenoble, France Unit for Virus Host Cell Interactions, Université Grenoble Alpes, Grenoble, France Unit for Virus Host Cell Interactions, CNRS, Grenoble, France
elife 3:e03653. 2014..cage between two Escherichia coli proteins with seemingly incompatible symmetries-the hexameric AAA+ ATPase RavA and the decameric inducible lysine decarboxylase LdcI-is reconstructed by cryo-electron microscopy to 11 Å ..