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From Proteopedia
Revision as of 16:23, 20 August 2014 by OCA (Talk | contribs)
A 3.3 MDa macromolecular cage between two E. 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 A resolution. Combined with a 7.5 A resolution reconstruction of the minimal complex between LdcI and the LdcI-binding domain of RavA, and the previously solved crystal structures of the individual components, this work enables to build a reliable pseudoatomic model of this unusual architecture and to identify conformational rearrangements and specific elements essential for complex formation. The design of the cage created via lateral interactions between five RavA rings is unique for the diverse AAA+ ATPase superfamily.
Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins.,Malet H, Liu K, El Bakkourri M, Chan SW, Effantin G, Bacia M, Houry WA, Gutsche I Elife. 2014 Aug 5:e03653. doi: 10.7554/eLife.03653. PMID:25097238[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Malet H, Liu K, El Bakkourri M, Chan SW, Effantin G, Bacia M, Houry WA, Gutsche I. Assembly principles of a unique cage formed by hexameric and decameric E. coli proteins. Elife. 2014 Aug 5:e03653. doi: 10.7554/eLife.03653. PMID:25097238 doi:http://dx.doi.org/10.7554/eLife.03653
