1m98: Difference between revisions

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New page: left|200px<br /><applet load="1m98" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m98, resolution 2.10Å" /> '''Crystal Structure of...
 
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[[Image:1m98.gif|left|200px]]<br /><applet load="1m98" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1m98.gif|left|200px]]<br /><applet load="1m98" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1m98, resolution 2.10&Aring;" />
caption="1m98, resolution 2.10&Aring;" />
'''Crystal Structure of Orange Carotenoid Protein'''<br />
'''Crystal Structure of Orange Carotenoid Protein'''<br />


==Overview==
==Overview==
Carotenoids undergo a wide range of photochemical reactions in animal, plant, and microbial systems. In photosynthetic organisms, in addition to, light harvesting, they perform an essential role in protecting against, light-induced damage by quenching singlet oxygen, superoxide anion, radicals, or triplet-state chlorophyll. We have determined the crystal, structure of a water-soluble orange carotenoid protein (OCP) isolated from, the cyanobacterium Arthrospira maxima at a resolution of 2.1 A. OCP forms, a homodimer with one carotenoid molecule per monomer. The carotenoid, binding site is lined by a striking number of methionine residues. The, structure reveals several possible ways in which the protein environment, influences the spectral properties of the pigment and provides insight, into how the OCP carries out its putative functions in photoprotection.
Carotenoids undergo a wide range of photochemical reactions in animal, plant, and microbial systems. In photosynthetic organisms, in addition to light harvesting, they perform an essential role in protecting against light-induced damage by quenching singlet oxygen, superoxide anion radicals, or triplet-state chlorophyll. We have determined the crystal structure of a water-soluble orange carotenoid protein (OCP) isolated from the cyanobacterium Arthrospira maxima at a resolution of 2.1 A. OCP forms a homodimer with one carotenoid molecule per monomer. The carotenoid binding site is lined by a striking number of methionine residues. The structure reveals several possible ways in which the protein environment influences the spectral properties of the pigment and provides insight into how the OCP carries out its putative functions in photoprotection.


==About this Structure==
==About this Structure==
1M98 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrospira_maxima Arthrospira maxima] with SUC, CL and HEQ as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M98 OCA].  
1M98 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arthrospira_maxima Arthrospira maxima] with <scene name='pdbligand=SUC:'>SUC</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=HEQ:'>HEQ</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M98 OCA].  


==Reference==
==Reference==
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[[Category: Arthrospira maxima]]
[[Category: Arthrospira maxima]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Kerfeld, C.A.]]
[[Category: Kerfeld, C A.]]
[[Category: Krogmann, D.]]
[[Category: Krogmann, D.]]
[[Category: Sawaya, M.R.]]
[[Category: Sawaya, M R.]]
[[Category: Vishnu, B.]]
[[Category: Vishnu, B.]]
[[Category: Yeates, T.O.]]
[[Category: Yeates, T O.]]
[[Category: CL]]
[[Category: CL]]
[[Category: HEQ]]
[[Category: HEQ]]
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[[Category: carotenoid binding protein]]
[[Category: carotenoid binding protein]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:15:01 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:52:53 2008''