1fgj | pdb_00001fgj
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X-RAY STRUCTURE OF HYDROXYLAMINE OXIDOREDUCTASE
Overview
The 2.8 A crystal structure of hydroxylamine oxidoreductase of a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea, is described. Twenty-four haems lie in the centre bottom of the trimeric molecule, localized in four clusters within each monomer. The haem clusters within the trimer are aligned to form a ring that has inlet and outlet sites. The inlet is occupied by a novel haem, P460, and there are two possible outlet sites per monomer formed by paired haems lying within a cavity or cleft on the protein surface. The structure suggests pathways by which electron transfer may occur through the precisely arranged haems and provides a framework for the interpretation of previous and future biochemical and genetic observations.
About this Structure
1FGJ is a Single protein structure of sequence from Nitrosomonas europaea with HEM and HEC as ligands. Active as Hydroxylamine oxidase, with EC number 1.7.3.4 Full crystallographic information is available from OCA.
Reference
The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea., Igarashi N, Moriyama H, Fujiwara T, Fukumori Y, Tanaka N, Nat Struct Biol. 1997 Apr;4(4):276-84. PMID:9095195
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