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2dre

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(New page: 200px<br /><applet load="2dre" size="350" color="white" frame="true" align="right" spinBox="true" caption="2dre, resolution 2.00&Aring;" /> '''Crystal structure of...)
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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17170107 17170107]
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17170107 17170107]
[[Category: Lepidium virginicum]]
[[Category: Lepidium virginicum]]
[[Category: Single protein]]
[[Category: Single protein]]
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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 Tue Jan 29 19:10:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:01:49 2008''

Revision as of 15:01, 21 February 2008

Image:2dre.jpg

2dre, resolution 2.00Å

Drag the structure with the mouse to rotate

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 with as ligand. 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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