Structure of RavA MoxR AAA+ protein reveals the design principles of a molecular cage modulating the inducible lysine decarboxylase activity.

Abstract:

:The MoxR family of AAA+ ATPases is widespread throughout bacteria and archaea but remains poorly characterized. 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 unique cage-like structure. Here, we present the X-ray structure of RavA and show that the αβα and all-α subdomains in the RavA AAA+ module are arranged as in magnesium chelatases rather than as in classical AAA+ proteins. RavA structure also contains a discontinuous triple-helical domain as well as a β-barrel-like domain forming a unique fold, which we termed the LARA domain. The LARA domain was found to mediate the interaction between RavA and LdcI. The RavA structure provides insights into how five RavA hexamers interact with two LdcI decamers to form the RavA-LdcI cage-like structure.

authors

El Bakkouri M,Gutsche I,Kanjee U,Zhao B,Yu M,Goret G,Schoehn G,Burmeister WP,Houry WA

doi

10.1073/pnas.1009092107

subject

Has Abstract

pub_date

2010-12-28 00:00:00

pages

22499-504

issue

52

eissn

0027-8424

issn

1091-6490

pii

1009092107

journal_volume

107

pub_type

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