1ft5
From Proteopedia
(New page: 200px<br /><applet load="1ft5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ft5, resolution 1.6Å" /> '''CRYSTAL STRUCTURE OF ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1ft5.jpg|left|200px]]<br /><applet load="1ft5" size=" | + | [[Image:1ft5.jpg|left|200px]]<br /><applet load="1ft5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ft5, resolution 1.6Å" /> | caption="1ft5, resolution 1.6Å" /> | ||
'''CRYSTAL STRUCTURE OF THE OXIDIZED STATE OF CYTOCHROME C554 FROM NITROSOMONAS EUROPAEA'''<br /> | '''CRYSTAL STRUCTURE OF THE OXIDIZED STATE OF CYTOCHROME C554 FROM NITROSOMONAS EUROPAEA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cytochrome c554 (cyt c554) is a tetra-heme cytochrome involved in the | + | 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== | ==About this Structure== | ||
| - | 1FT5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Nitrosomonas_europaea Nitrosomonas europaea] with PO4 and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1FT5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Nitrosomonas_europaea Nitrosomonas europaea] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FT5 OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Nitrosomonas europaea]] | [[Category: Nitrosomonas europaea]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Arciero, D | + | [[Category: Arciero, D M.]] |
| - | [[Category: Hooper, A | + | [[Category: Hooper, A B.]] |
| - | [[Category: Iverson, T | + | [[Category: Iverson, T M.]] |
| - | [[Category: Rees, D | + | [[Category: Rees, D C.]] |
[[Category: HEM]] | [[Category: HEM]] | ||
[[Category: PO4]] | [[Category: PO4]] | ||
[[Category: heme-stacking]] | [[Category: heme-stacking]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:20 2008'' |
Revision as of 10:42, 21 February 2008
|
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 with and as ligands. 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 Thu Feb 21 12:42:20 2008
