1zrr
From Proteopedia
Residual Dipolar Coupling Refinement of Acireductone Dioxygenase from Klebsiella
Overview
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.
About this Structure
1ZRR is a Single protein structure of sequence from Klebsiella oxytoca. This structure supersedes the now removed PDB entry 1m4o. Full crystallographic information is available from OCA.
Reference
A refined model for the structure of acireductone dioxygenase from Klebsiella ATCC 8724 incorporating residual dipolar couplings., Pochapsky TC, Pochapsky SS, Ju T, Hoefler C, Liang J, J Biomol NMR. 2006 Feb;34(2):117-27. PMID:16518698 Page seeded by OCA on Sat May 3 17:59:24 2008
