This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ft5
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1ft5 |SIZE=350|CAPTION= <scene name='initialview01'>1ft5</scene>, resolution 1.6Å | |PDB= 1ft5 |SIZE=350|CAPTION= <scene name='initialview01'>1ft5</scene>, resolution 1.6Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1bvb|1BVB]], [[1ft6|1FT6]] | ||
| + | |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> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Iverson, T M.]] | [[Category: Iverson, T M.]] | ||
[[Category: Rees, D C.]] | [[Category: Rees, D C.]] | ||
| - | [[Category: HEM]] | ||
| - | [[Category: PO4]] | ||
[[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 20:29:56 2008'' |
Revision as of 17:29, 30 March 2008
| |||||||
| , resolution 1.6Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1BVB, 1FT6
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 20:29:56 2008
