1ft6: Difference between revisions
New page: left|200px<br /><applet load="1ft6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ft6, resolution 1.8Å" /> '''REDUCED STATE OF CYTO... |
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[[Image:1ft6.jpg|left|200px]]<br /><applet load="1ft6" size=" | [[Image:1ft6.jpg|left|200px]]<br /><applet load="1ft6" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ft6, resolution 1.8Å" /> | caption="1ft6, resolution 1.8Å" /> | ||
'''REDUCED STATE OF CYTOCHROME C554 FROM NITROSOMONAS EUROPAEA'''<br /> | '''REDUCED 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== | ||
1FT6 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 SO3, PO4, HEM and DTN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1FT6 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=SO3:'>SO3</scene>, <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=DTN:'>DTN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FT6 OCA]. | ||
==Reference== | ==Reference== | ||
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[[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: DTN]] | [[Category: DTN]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
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[[Category: heme-stacking]] | [[Category: heme-stacking]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:26 2008'' | ||
Revision as of 10:42, 21 February 2008
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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 with SO3, PO4, HEM and DTN 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
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