1cfm

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|PDB= 1cfm |SIZE=350|CAPTION= <scene name='initialview01'>1cfm</scene>, resolution 2.00&Aring;
|PDB= 1cfm |SIZE=350|CAPTION= <scene name='initialview01'>1cfm</scene>, resolution 2.00&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene>
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cfm OCA], [http://www.ebi.ac.uk/pdbsum/1cfm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cfm RCSB]</span>
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[[Category: Malkin, R.]]
[[Category: Malkin, R.]]
[[Category: Zhang, Z.]]
[[Category: Zhang, Z.]]
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[[Category: HEM]]
 
[[Category: cytochrome f]]
[[Category: cytochrome f]]
[[Category: electron transport]]
[[Category: electron transport]]
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[[Category: proton wire]]
[[Category: proton wire]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:23:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:20:43 2008''

Revision as of 16:20, 30 March 2008


PDB ID 1cfm

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CYTOCHROME F FROM CHLAMYDOMONAS REINHARDTII


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.

About this Structure

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

Reference

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

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