1ft6: Difference between revisions

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{{STRUCTURE_1ft6|  PDB=1ft6  |  SCENE=  }}  
{{STRUCTURE_1ft6|  PDB=1ft6  |  SCENE=  }}  


'''REDUCED STATE OF CYTOCHROME C554 FROM NITROSOMONAS EUROPAEA'''
===REDUCED STATE OF CYTOCHROME C554 FROM NITROSOMONAS EUROPAEA===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Rees, D C.]]
[[Category: Rees, D C.]]
[[Category: Heme-stacking]]
[[Category: Heme-stacking]]
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