1ZRR

Residual Dipolar Coupling Refinement of Acireductone Dioxygenase from Klebsiella

Replaces:  1M4O

Summary for 1ZRR

• Entry DOI: 10.2210/pdb1zrr/pdb
• Related: 1M4O
• NMR Information: BMRB: 4313
• Descriptor: E-2/E-2' protein, NICKEL (II) ION (3 entities in total)
• Functional Keywords: nickel, cupin, beta helix, methionine salvage, oxidoreductase
• Biological source: Klebsiella oxytoca
• Total number of polymer chains: 1
• Total formula weight: 20278.10

Authors

Pochapsky, T.C.,Pochapsky, S.S.,Ju, T.,Hoefler, C.,Liang, J. (deposition date: 2005-05-19, release date: 2005-12-06, Last modification date: 2024-05-22)

Primary citation

Pochapsky, T.C.,Pochapsky, S.S.,Ju, T.,Hoefler, C.,Liang, J.
A refined model for the structure of acireductone dioxygenase from Klebsiella ATCC 8724 incorporating residual dipolar couplings
J.Biomol.NMR, 34:117-127, 2006

PubMed 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.

PubMed: 16518698
DOI: 10.1007/s10858-005-5735-8

Experimental method

SOLUTION NMR