1ft5: Difference between revisions

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[[Image:1ft5.jpg|left|200px]]<br /><applet load="1ft5" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1ft5.jpg|left|200px]]<br /><applet load="1ft5" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1ft5, resolution 1.6Å" />

'''CRYSTAL STRUCTURE OF THE OXIDIZED STATE OF CYTOCHROME C554 FROM NITROSOMONAS EUROPAEA'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1FT5 OCA].

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==

Line 13:

[[Category: Nitrosomonas europaea]]

[[Category: Single protein]]

[[Category: Arciero, D.M.]]

[[Category: Arciero, D M.]]

[[Category: Hooper, A.B.]]

[[Category: Hooper, A B.]]

[[Category: Iverson, T.M.]]

[[Category: Iverson, T M.]]

[[Category: Rees, D.C.]]

[[Category: Rees, D C.]]

[[Category: HEM]]

[[Category: PO4]]

[[Category: heme-stacking]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 15~~:15:~~15 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:20 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1ft5.jpg|left|200px]]<br /><applet load="1ft5" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ft5.jpg|left|200px]]<br /><applet load="1ft5" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ft5, resolution 1.6&Aring;" />
 '''CRYSTAL STRUCTURE OF THE OXIDIZED STATE OF CYTOCHROME C554 FROM NITROSOMONAS EUROPAEA'''<br />
 ==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.
+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==
-FT5 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FT5 OCA].
+FT5 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==
@@ Line 13: / Line 13: @@
 [[Category: Nitrosomonas europaea]]
 [[Category: Single protein]]
-[[Category: Arciero, D.M.]]
+[[Category: Arciero, D M.]]
-[[Category: Hooper, A.B.]]
+[[Category: Hooper, A B.]]
-[[Category: Iverson, T.M.]]
+[[Category: Iverson, T M.]]
-[[Category: Rees, D.C.]]
+[[Category: Rees, D C.]]
 [[Category: HEM]]
 [[Category: PO4]]
 [[Category: heme-stacking]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:15:15 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:20 2008''