1ft6: Difference between revisions

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[[Image:1ft6.jpg|left|200px]]
[[Image:1ft6.jpg|left|200px]]


{{Structure
<!--
|PDB= 1ft6 |SIZE=350|CAPTION= <scene name='initialview01'>1ft6</scene>, resolution 1.8&Aring;
The line below this paragraph, containing "STRUCTURE_1ft6", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=DTN:DITHIONITE'>DTN</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO3:SULFITE+ION'>SO3</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY=
or leave the SCENE parameter empty for the default display.
|GENE=
-->
|DOMAIN=
{{STRUCTURE_1ft6|  PDB=1ft6 |  SCENE= }}  
|RELATEDENTRY=[[1ft5|1FT5]], [[1bvb|1BVB]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ft6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ft6 OCA], [http://www.ebi.ac.uk/pdbsum/1ft6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ft6 RCSB]</span>
}}


'''REDUCED STATE OF CYTOCHROME C554 FROM NITROSOMONAS EUROPAEA'''
'''REDUCED 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.]]
[[Category: heme-stacking]]
[[Category: Heme-stacking]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:44:20 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:29:52 2008''

Revision as of 16:44, 2 May 2008

File:1ft6.jpg

Template:STRUCTURE 1ft6

REDUCED STATE OF CYTOCHROME C554 FROM NITROSOMONAS EUROPAEA


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 Page seeded by OCA on Fri May 2 16:44:20 2008

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