A Structural Model of the Urease Activation Complex Derived from Ion Mobility-Mass Spectrometry and Integrative Modeling.

ABSTRACT: The synthesis of active Klebsiella aerogenes urease via an 18-subunit enzyme apoprotein-accessory protein pre-activation complex has been well studied biochemically, but thus far this complex has remained refractory to direct structural characterization. Using ion mobility-mass spectrometry, we characterized several protein complexes between the core urease apoprotein and its accessory proteins, including the 610-kDa (UreABC)₃(UreDFG)₃ complex. Using our recently developed computational modeling workflow, we generated ensembles of putative (UreABC)₃(UreDFG)₃ species consistent with experimental restraints and characterized the structural ambiguity present in these models. By integrating structural information from previous studies, we increased t

SUBMITTER: Eschweiler JD 

PROVIDER: S-EPMC5884726 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature