Journal
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
Volume 480, Issue 1, Pages 51-57Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2008.09.004
Keywords
Urease; Activation; Flexibility; Small-angle X-ray scattering
Categories
Funding
- National Institutes of Health [DK45686, GM67249]
- MSU Quantitative Biology and Modeling Initiative [71-4841, KP1102010]
- office of Biological and Environmental Research of the U.S. Department of Energy, [DE-AC05-000R22725]
- Oak Ridge National Laboratory
- UT-Batelle, LLC
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Conformational changes of Klebsiella aerogenes urease apoprotein (UreABC)(3) induced upon binding of the UreD and UreF accessory proteins were examined by a combination of flexibility analysis, mutagenesis, and small-angle X-ray scattering (SANS). ProFlex analysis of urease provided evidence that the major domain of UreB can move in a hinge-like motion to account for prior chemical cross-linking results. Rigidification of the UreB hinge region, accomplished through a G I I P mutation, reduced the extent of urease activation, in part by decreasing the nickel content of the mutant enzyme, and by sequestering a portion of the urease apoprotein in a novel activation complex that includes all of the accessory proteins. SAXS analyses of urease, (UreABC-UreD)(3), and (UreABC-UreDF)(3) confirm that UreD and UreF bind near UreB at the periphery of the (UreAC)(3) Structure. This study supports an activation model in which a domain-shifted UreB conformation in (UreABC-UreDF)3 allows CO2 and nickel ions to gain access to the nascent active site. (C) 2008 Elsevier Inc. All rights reserved.
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