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• W2048261544 endingPage "127" @default.
• W2048261544 startingPage "117" @default.
• W2048261544 abstract "Acireductone dioxygenase (ARD) from Klebsiella ATCC 8724 is a metalloenzyme that is capable of catalyzing different reactions with the same substrates (acireductone and O2) depending upon the metal bound in the active site. A model for the solution structure of the paramagnetic Ni2+-containing ARD has been refined using residual dipolar couplings (RDCs) measured in two media. Additional dihedral restraints based on chemical shift (TALOS) were included in the refinement, and backbone structure in the vicinity of the active site was modeled from a crystallographic structure of the mouse homolog of ARD. The incorporation of residual dipolar couplings into the structural refinement alters the relative orientations of several structural features significantly, and improves local secondary structure determination. Comparisons between the solution structures obtained with and without RDCs are made, and structural similarities and differences between mouse and bacterial enzymes are described. Finally, the biological significance of these differences is considered." @default.
• W2048261544 created "2016-06-24" @default.
• W2048261544 creator A5002587886 @default.
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• W2048261544 creator A5052965284 @default.
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• W2048261544 creator A5074947482 @default.
• W2048261544 date "2006-02-01" @default.
• W2048261544 modified "2023-10-12" @default.
• W2048261544 title "A Refined Model for the Structure of Acireductone Dioxygenase from Klebsiella ATCC 8724 Incorporating Residual Dipolar Couplings" @default.
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• W2048261544 doi "https://doi.org/10.1007/s10858-005-5735-8" @default.
• W2048261544 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1661621" @default.
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• W2048261544 hasPublicationYear "2006" @default.
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