1fgj
From Proteopedia
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| , resolution 2.8Å | |||||||
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| Ligands: | , | ||||||
| Activity: | Hydroxylamine oxidase, with EC number 1.7.3.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Sun Mar 30 20:22:25 2008
