1ppr: Difference between revisions

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[[Image:1ppr.gif|left|200px]]<br /><applet load="1ppr" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1ppr.gif|left|200px]]<br /><applet load="1ppr" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1ppr, resolution 2.0Å" />

'''PERIDININ-CHLOROPHYLL-PROTEIN OF AMPHIDINIUM CARTERAE'''<br />

==Overview==

Peridinin-chlorophyll-protein, a water-soluble light-harvesting complex, that has a blue-green absorbing carotenoid as its main pigment, is present, in most photosynthetic dinoflagellates. Its high-resolution (2.0 angstrom), x-ray structure reveals a noncrystallographic trimer in which each, polypeptide contains an unusual jellyroll fold of the alpha-helical amino-, and carboxyl-terminal domains. These domains constitute a scaffold with, pseudo-twofold symmetry surrounding a hydrophobic cavity filled by two, lipid, eight peridinin, and two chlorophyll a molecules. The structural, basis for efficient excitonic energy transfer from peridinin to, chlorophyll is found in the clustering of peridinins around the, chlorophylls at van der Waals distances.

Peridinin-chlorophyll-protein, a water-soluble light-harvesting complex that has a blue-green absorbing carotenoid as its main pigment, is present in most photosynthetic dinoflagellates. Its high-resolution (2.0 angstrom) x-ray structure reveals a noncrystallographic trimer in which each polypeptide contains an unusual jellyroll fold of the alpha-helical amino- and carboxyl-terminal domains. These domains constitute a scaffold with pseudo-twofold symmetry surrounding a hydrophobic cavity filled by two lipid, eight peridinin, and two chlorophyll a molecules. The structural basis for efficient excitonic energy transfer from peridinin to chlorophyll is found in the clustering of peridinins around the chlorophylls at van der Waals distances.

==About this Structure==

1PPR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Amphidinium_carterae Amphidinium carterae] with CLA, PID and DGD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1PPR OCA].

1PPR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Amphidinium_carterae Amphidinium carterae] with <scene name='pdbligand=CLA:'>CLA</scene>, <scene name='pdbligand=PID:'>PID</scene> and <scene name='pdbligand=DGD:'>DGD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PPR OCA].

==Reference==

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[[Category: photosynthesis]]

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@@ Line 1: / Line 1: @@
-[[Image:1ppr.gif|left|200px]]<br /><applet load="1ppr" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ppr.gif|left|200px]]<br /><applet load="1ppr" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1ppr, resolution 2.0&Aring;" />
 '''PERIDININ-CHLOROPHYLL-PROTEIN OF AMPHIDINIUM CARTERAE'''<br />
 ==Overview==
-Peridinin-chlorophyll-protein, a water-soluble light-harvesting complex, that has a blue-green absorbing carotenoid as its main pigment, is present, in most photosynthetic dinoflagellates. Its high-resolution (2.0 angstrom), x-ray structure reveals a noncrystallographic trimer in which each, polypeptide contains an unusual jellyroll fold of the alpha-helical amino-, and carboxyl-terminal domains. These domains constitute a scaffold with, pseudo-twofold symmetry surrounding a hydrophobic cavity filled by two, lipid, eight peridinin, and two chlorophyll a molecules. The structural, basis for efficient excitonic energy transfer from peridinin to, chlorophyll is found in the clustering of peridinins around the, chlorophylls at van der Waals distances.
+Peridinin-chlorophyll-protein, a water-soluble light-harvesting complex that has a blue-green absorbing carotenoid as its main pigment, is present in most photosynthetic dinoflagellates. Its high-resolution (2.0 angstrom) x-ray structure reveals a noncrystallographic trimer in which each polypeptide contains an unusual jellyroll fold of the alpha-helical amino- and carboxyl-terminal domains. These domains constitute a scaffold with pseudo-twofold symmetry surrounding a hydrophobic cavity filled by two lipid, eight peridinin, and two chlorophyll a molecules. The structural basis for efficient excitonic energy transfer from peridinin to chlorophyll is found in the clustering of peridinins around the chlorophylls at van der Waals distances.
 ==About this Structure==
-PPR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Amphidinium_carterae Amphidinium carterae] with CLA, PID and DGD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PPR OCA].
+PPR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Amphidinium_carterae Amphidinium carterae] with <scene name='pdbligand=CLA:'>CLA</scene>, <scene name='pdbligand=PID:'>PID</scene> and <scene name='pdbligand=DGD:'>DGD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PPR OCA].
 ==Reference==
@@ Line 24: / Line 24: @@
 [[Category: photosynthesis]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:00:28 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:31:13 2008''