1ZRR

Residual Dipolar Coupling Refinement of Acireductone Dioxygenase from Klebsiella

「1M4O」から置き換えられました

1ZRR の概要

• エントリーDOI: 10.2210/pdb1zrr/pdb
• 関連するPDBエントリー: 1M4O
• NMR情報: BMRB: 4313
• 分子名称: E-2/E-2' protein, NICKEL (II) ION (3 entities in total)
• 機能のキーワード: nickel, cupin, beta helix, methionine salvage, oxidoreductase
• 由来する生物種: Klebsiella oxytoca
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20278.10

構造登録者

Pochapsky, T.C.,Pochapsky, S.S.,Ju, T.,Hoefler, C.,Liang, J. (登録日: 2005-05-19, 公開日: 2005-12-06, 最終更新日: 2024-05-22)

主引用文献

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

実験手法

SOLUTION NMR