4FAS

Complex crystal structure of hydroxylamine oxidoreductase and NE1300 from Nitrosomonas europaea

4FAS の概要

• エントリーDOI: 10.2210/pdb4fas/pdb
• 分子名称: Hydroxylamine oxidoreductase, NITRATE ION, NE1300, ... (11 entities in total)
• 機能のキーワード: hydroxylamine oxidation, heme c binding, oxidoreductase
• 由来する生物種: Nitrosomonas europaea; 詳細
• 細胞内の位置: Periplasm: Q50925
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 226146.85

構造登録者

Cedervall, P.E.,Wilmot, C.M. (登録日: 2012-05-22, 公開日: 2013-09-04, 最終更新日: 2024-11-06)

主引用文献

Cedervall, P.E.,Hooper, A.B.,Wilmot, C.M.
Structural studies of hydroxylamine oxidoreductase reveal a unique heme cofactor and a previously unidentified interaction partner.
Biochemistry, 52:6211-6218, 2013

PubMed Abstract: Hydroxylamine oxidoreductase (HAO) is a 24-heme homotrimeric enzyme that catalyzes the conversion of hydroxylamine to nitrite in nitrifying bacteria: a key reaction in the nitrogen cycle. One heme in each HAO monomer is a highly unusual heme P460 that is the site of catalysis. This was proposed to be a c-type heme that contained an additional porphyrin-tyrosine cross-link. Here, we report the crystal structure of HAO from Nitrosomonas europaea to 2.1 Å resolution that defines a different model compatible with the crystallographic and biochemical data. The structure reveals that heme P460 contains two covalent cross-links between the porphyrin and a Tyr residue. In addition, the enzyme was purified from source, and an unknown physiological HAO binding partner was present within the crystal (annotated in the genome as hypothetical protein NE1300). NE1300 may play a structural role in the ternary complex with cytochrome c554, the physiological electron acceptor of HAO.

PubMed: 23952581
DOI: 10.1021/bi400960w

実験手法

X-RAY DIFFRACTION (2.1 Å)