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.
journal_name
Proc Natl Acad Sci U S Aauthors
El Bakkouri M,Gutsche I,Kanjee U,Zhao B,Yu M,Goret G,Schoehn G,Burmeister WP,Houry WAdoi
10.1073/pnas.1009092107subject
Has Abstractpub_date
2010-12-28 00:00:00pages
22499-504issue
52eissn
0027-8424issn
1091-6490pii
1009092107journal_volume
107pub_type
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