1ft5

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[[Image:1ft5.jpg|left|200px]]
[[Image:1ft5.jpg|left|200px]]
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{{Structure
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|PDB= 1ft5 |SIZE=350|CAPTION= <scene name='initialview01'>1ft5</scene>, resolution 1.6&Aring;
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The line below this paragraph, containing "STRUCTURE_1ft5", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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{{STRUCTURE_1ft5| PDB=1ft5 | SCENE= }}
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|RELATEDENTRY=[[1bvb|1BVB]], [[1ft6|1FT6]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ft5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ft5 OCA], [http://www.ebi.ac.uk/pdbsum/1ft5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ft5 RCSB]</span>
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'''CRYSTAL STRUCTURE OF THE OXIDIZED STATE OF CYTOCHROME C554 FROM NITROSOMONAS EUROPAEA'''
'''CRYSTAL STRUCTURE OF THE OXIDIZED STATE OF CYTOCHROME C554 FROM NITROSOMONAS EUROPAEA'''
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[[Category: Iverson, T M.]]
[[Category: Iverson, T M.]]
[[Category: Rees, D C.]]
[[Category: Rees, D C.]]
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[[Category: heme-stacking]]
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[[Category: Heme-stacking]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:44:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:29:56 2008''
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Revision as of 13:44, 2 May 2008

Template:STRUCTURE 1ft5

CRYSTAL STRUCTURE OF THE OXIDIZED STATE OF CYTOCHROME C554 FROM NITROSOMONAS EUROPAEA


Overview

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 Structure

1FT5 is a Single protein structure of sequence from Nitrosomonas europaea. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 16:44:15 2008

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