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2dre

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|PDB= 2dre |SIZE=350|CAPTION= <scene name='initialview01'>2dre</scene>, resolution 2.00&Aring;
|PDB= 2dre |SIZE=350|CAPTION= <scene name='initialview01'>2dre</scene>, resolution 2.00&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CLA:CHLOROPHYLL A'>CLA</scene>
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|LIGAND= <scene name='pdbligand=CLA:CHLOROPHYLL+A'>CLA</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=2dre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dre OCA], [http://www.ebi.ac.uk/pdbsum/2dre PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dre RCSB]</span>
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[[Category: Satoh, H.]]
[[Category: Satoh, H.]]
[[Category: Uchida, A.]]
[[Category: Uchida, A.]]
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[[Category: CLA]]
 
[[Category: beta-trefoil]]
[[Category: beta-trefoil]]
[[Category: chlorophyll]]
[[Category: chlorophyll]]
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[[Category: water-soluble chlorophyll protein]]
[[Category: water-soluble chlorophyll protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:30:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:38:27 2008''

Revision as of 23:38, 30 March 2008

Image:2dre.jpg


PDB ID 2dre

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



Crystal structure of Water-soluble chlorophyll protein from lepidium virginicum at 2.00 angstrom resolution


Overview

A water-soluble chlorophyll-binding protein (WSCP) is the single known instance of a putative chlorophyll (Chl) carrier in green plants. Recently the photoprotective function of WSCP has been demonstrated by EPR measurements; the light-induced singlet-oxygen formation of Chl in the WSCP tetramer is about four times lower than that of unbound Chl. This paper describes the crystal structure of the WSCP-Chl complex purified from leaves of Lepidium virginicum (Virginia pepperweed) to clarify the mechanism of its photoprotective function. The WSCP-Chl complex is a homotetramer comprising four protein chains of 180 amino acids and four Chl molecules. At the center of the complex one hydrophobic cavity is formed in which all of the four Chl molecules are tightly packed and isolated from bulk solvent. With reference to the novel Chl-binding mode, we propose that the photoprotection mechanism may be based on the inhibition of physical contact between the Chl molecules and molecular oxygen.

About this Structure

2DRE is a Single protein structure of sequence from Lepidium virginicum. Full crystallographic information is available from OCA.

Reference

Structural mechanism and photoprotective function of water-soluble chlorophyll-binding protein., Horigome D, Satoh H, Itoh N, Mitsunaga K, Oonishi I, Nakagawa A, Uchida A, J Biol Chem. 2007 Mar 2;282(9):6525-31. Epub 2006 Dec 14. PMID:17170107

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