A refined model for the structure of acireductone dioxygenase from Klebsiella ATCC 8724 incorporating residual dipolar couplings

Journal of Biomolecular NMR
T C PochapskyJue Liang

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.

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Citations

Oct 31, 2008·Inorganic Chemistry·Katarzyna RudzkaLisa M Berreau
Jun 30, 2011·The Journal of Biological Chemistry·Erin J FriedmanAlan M Jones
Sep 17, 2013·Archives of Biochemistry and Biophysics·Jodi L BoerRobert P Hausinger
Jan 11, 2007·Genes to Cells : Devoted to Molecular & Cellular Mechanisms·Isamu GotohMotoharu Seiki
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May 18, 2013·Journal of Molecular Biology·Manuel SpartaAnastassia N Alexandrova
Sep 6, 2007·Neoplasia : an International Journal for Oncology Research·Shane W OramZhou Wang
Jul 22, 2017·Chemical Reviews·Aditi R DeshpandeDagmar Ringe
Jun 6, 2018·Physical Chemistry Chemical Physics : PCCP·Wen-Juan WangRong-Zhen Liao
Feb 6, 2020·Protein Science : a Publication of the Protein Society·Marila Alfano, Christine Cavazza
Aug 29, 2009·Chemical Reviews·Yanjie Li, Deborah B Zamble

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