4upf
Assembly principles of the unique cage formed by the ATPase RavA hexamer and the lysine decarboxylase LdcI decamerAssembly principles of the unique cage formed by the ATPase RavA hexamer and the lysine decarboxylase LdcI decamer
Structural highlights
Function[LDCI_ECOLI] Plays a role in pH homeostasis by consuming protons and neutralizing the acidic by-products of carbohydrate fermentation. [RAVA_ECOLI] Functions as an ATPase. May play a role in metal insertion (metal-chelatase) or as a chaperone.[HAMAP-Rule:MF_01625] Publication Abstract from PubMedA 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. See AlsoReferences
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