1ft6
From Proteopedia
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|PDB= 1ft6 |SIZE=350|CAPTION= <scene name='initialview01'>1ft6</scene>, resolution 1.8Å | |PDB= 1ft6 |SIZE=350|CAPTION= <scene name='initialview01'>1ft6</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |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> | ||
}} | }} | ||
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[[Category: Iverson, T M.]] | [[Category: Iverson, T M.]] | ||
[[Category: Rees, D C.]] | [[Category: Rees, D C.]] | ||
| - | [[Category: DTN]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: PO4]] | ||
| - | [[Category: SO3]] | ||
[[Category: heme-stacking]] | [[Category: heme-stacking]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:29:52 2008'' |
Revision as of 17:29, 30 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Related: | 1FT5, 1BVB
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
REDUCED 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
1FT6 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
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