1cfm: Difference between revisions

Revision as of 13:05, 21 February 2008

CYTOCHROME F FROM CHLAMYDOMONAS REINHARDTII

OverviewOverview

A truncated form of cytochrome f from Chlamydomonas reinhardtii (an important eukaryotic model organism for photosynthetic electron transfer studies) has been crystallized (space group P2(1)2(1)2(1); three molecules/asymmetric unit) and its structure determined to 2.0 A resolution by molecular replacement using the coordinates of a truncated turnip cytochrome f as a model. The structure displays the same folding and detailed features as turnip cytochrome f, including (a) an unusual heme Fe ligation by the alpha-amino group of tyrosine 1, (b) a cluster of lysine residues (proposed docking site of plastocyanin), and (c) the presence of a chain of seven water molecules bound to conserved residues and extending between the heme pocket and K58 and K66 at the lysine cluster. For this array of waters, we propose a structural role. Two cytochrome f molecules are related by a noncrystallographic symmetry operator which is a distorted proper 2-fold rotation. This may represent the dimeric relation of the monomers in situ; however, the heme orientation suggested by this model is not consistent with previous EPR measurements on oriented membranes.

About this StructureAbout this Structure

1CFM is a Single protein structure of sequence from Chlamydomonas reinhardtii with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

X-ray structure of a truncated form of cytochrome f from chlamydomonas reinhardtii., Chi YI, Huang LS, Zhang Z, Fernandez-Velasco JG, Berry EA, Biochemistry. 2000 Jul 4;39(26):7689-701. PMID:10869174

Page seeded by OCA on Thu Feb 21 12:05:34 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1cfm.jpg|left|200px]]<br /><applet load="1cfm" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1cfm.jpg|left|200px]]<br /><applet load="1cfm" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1cfm, resolution 2.00&Aring;" />
 '''CYTOCHROME F FROM CHLAMYDOMONAS REINHARDTII'''<br />
 ==Overview==
-A truncated form of cytochrome f from Chlamydomonas reinhardtii (an, important eukaryotic model organism for photosynthetic electron transfer, studies) has been crystallized (space group P2(1)2(1)2(1); three, molecules/asymmetric unit) and its structure determined to 2.0 A, resolution by molecular replacement using the coordinates of a truncated, turnip cytochrome f as a model. The structure displays the same folding, and detailed features as turnip cytochrome f, including (a) an unusual, heme Fe ligation by the alpha-amino group of tyrosine 1, (b) a cluster of, lysine residues (proposed docking site of plastocyanin), and (c) the, presence of a chain of seven water molecules bound to conserved residues, and extending between the heme pocket and K58 and K66 at the lysine, cluster. For this array of waters, we propose a structural role. Two, cytochrome f molecules are related by a noncrystallographic symmetry, operator which is a distorted proper 2-fold rotation. This may represent, the dimeric relation of the monomers in situ; however, the heme, orientation suggested by this model is not consistent with previous EPR, measurements on oriented membranes.
+A truncated form of cytochrome f from Chlamydomonas reinhardtii (an important eukaryotic model organism for photosynthetic electron transfer studies) has been crystallized (space group P2(1)2(1)2(1); three molecules/asymmetric unit) and its structure determined to 2.0 A resolution by molecular replacement using the coordinates of a truncated turnip cytochrome f as a model. The structure displays the same folding and detailed features as turnip cytochrome f, including (a) an unusual heme Fe ligation by the alpha-amino group of tyrosine 1, (b) a cluster of lysine residues (proposed docking site of plastocyanin), and (c) the presence of a chain of seven water molecules bound to conserved residues and extending between the heme pocket and K58 and K66 at the lysine cluster. For this array of waters, we propose a structural role. Two cytochrome f molecules are related by a noncrystallographic symmetry operator which is a distorted proper 2-fold rotation. This may represent the dimeric relation of the monomers in situ; however, the heme orientation suggested by this model is not consistent with previous EPR measurements on oriented membranes.
 ==About this Structure==
-CFM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CFM OCA].
+CFM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CFM OCA].
 ==Reference==
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 [[Category: Chlamydomonas reinhardtii]]
 [[Category: Single protein]]
-[[Category: Berry, E.A.]]
+[[Category: Berry, E A.]]
-[[Category: Chi, Y.I.]]
+[[Category: Chi, Y I.]]
-[[Category: Fernandez-Velasco, J.G.]]
+[[Category: Fernandez-Velasco, J G.]]
-[[Category: Huang, L.S.]]
+[[Category: Huang, L S.]]
 [[Category: Malkin, R.]]
 [[Category: Zhang, Z.]]
@@ Line 26: / Line 26: @@
 [[Category: proton wire]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:25:00 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:05:34 2008''