4n4l | pdb_00004n4l

Kuenenia stuttgartiensis hydroxylamine oxidoreductase soaked in hydrazine

spinqualitylabelsall models 4n4l, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4n4l is a 1 chain structure with sequence from Candidatus Kuenenia stuttgartiensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, HEC, HG1, HZN, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q1PX48_KUEST Publication Abstract from PubMed Nitric oxide (NO) is an important molecule in all domains of life with significant biological functions in both pro- and eukaryotes. Anaerobic ammonium-oxidizing (anammox) bacteria that contribute substantially to the release of fixed nitrogen into the atmosphere use the oxidizing power of NO to activate inert ammonium into hydrazine (N2H4). Here, we describe an enzyme from the anammox bacterium Kuenenia stuttgartiensis that uses a novel pathway to make NO from hydroxylamine. This new enzyme is related to octaheme hydroxylamine oxidoreductase (HAO), a key protein in aerobic ammonium-oxidizing bacteria. By a multiphasic approach including the determination of the crystal structure of the K. stuttgartiensis enzyme at 1.8Angstrom resolution and refinement and reassessment of the HAO structure from Nitrosomonas europaea, both in the presence and absence of their substrates, we propose a model for NO formation by the K. stuttgartiensis enzyme. Our results expand the understanding of the functions that the widespread family of octaheme proteins have. Structural basis of biological NO generation by octaheme oxidoreductases.,Maalcke WJ, Dietl A, Marritt SJ, Butt JN, Jetten MS, Keltjens JT, Barends TR, Kartal B J Biol Chem. 2013 Dec 3. PMID:24302732 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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