1ft6
REDUCED STATE OF CYTOCHROME C554 FROM NITROSOMONAS EUROPAEA
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| , resolution 1.8Å | |||||||
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| Ligands: | , , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
Cytochrome c554 (cyt c554) is a tetra-heme cytochrome involved in the oxidation of NH3 by Nitrosomonas europaea. The X-ray crystal structures of both the oxidized and dithionite-reduced states of cyt c554 in a new, rhombohedral crystal form have been solved by molecular replacement, at 1.6 A and 1.8 A resolution, respectively. Upon reduction, the conformation of the polypeptide chain changes between residues 175 and 179, which are adjacent to hemes III and IV. Cyt c554 displays conserved heme-packing motifs that are present in other heme-containing proteins. Comparisons to hydroxylamine oxidoreductase, the electron donor to cyt c554, and cytochrome c nitrite reductase, an enzyme involved in nitrite ammonification, reveal substantial structural similarity in the polypeptide chain surrounding the heme core environment. The structural determinants of these heme-packing motifs extend to the buried water molecules that hydrogen bond to the histidine ligands to the heme iron. In the original structure determination of a tetragonal crystal form, a cis peptide bond between His129 and Phe130 was identified that appeared to be stabilized by crystal contacts. In the rhombohedral crystal form used in the present high-resolution structure determination, this peptide bond adopts the trans conformation, but with disallowed angles of phi and psi.
About this StructureAbout this Structure
1FT6 is a Single protein structure of sequence from Nitrosomonas europaea. Full crystallographic information is available from OCA.
ReferenceReference
High-resolution structures of the oxidized and reduced states of cytochrome c554 from Nitrosomonas europaea., Iverson TM, Arciero DM, Hooper AB, Rees DC, J Biol Inorg Chem. 2001 Apr;6(4):390-7. PMID:11372197
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