1b8d

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(New page: 200px<br /><applet load="1b8d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b8d, resolution 1.90&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1b8d.gif|left|200px]]<br /><applet load="1b8d" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1b8d, resolution 1.90&Aring;" />
caption="1b8d, resolution 1.90&Aring;" />
'''CRYSTAL STRUCTURE OF A PHYCOUROBILIN-CONTAINING PHYCOERYTHRIN'''<br />
'''CRYSTAL STRUCTURE OF A PHYCOUROBILIN-CONTAINING PHYCOERYTHRIN'''<br />
==Overview==
==Overview==
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The structure of R-phycoerythrin (R-PE) from the red alga Griffithsia, monilis was solved at 1.90-A resolution by molecular replacement, using, the atomic coordinates of cyanobacterial phycocyanin from Fremyella, diplosiphon as a model. The crystallographic R factor for the final model, is 17.5% (Rfree 22.7%) for reflections in the range 100-1.90 A. The model, consists of an (alphabeta)2 dimer with an internal noncrystallographic, dyad and a fragment of the gamma-polypeptide. The alpha-polypeptide (164, amino acid residues) has two covalently bound phycoerythrobilins at, positions alpha82 and alpha139. The beta-polypeptide (177 residues) has, two phycoerythrobilins bound to residues beta82 and beta158 and one, phycourobilin covalently attached to rings A and D at residues beta50 and, beta61, respectively. The electron density of the gamma-polypeptide is, mostly averaged out by threefold crystallographic symmetry, but a, dipeptide (Gly-Tyr) and one single Tyr could be modeled. These two, tyrosine residues of the gamma-polypeptide are in close proximity to the, phycoerythrobilins at position beta82 of two symmetry-related, beta-polypeptides and are related by the same noncrystallographic dyad as, the (alphabeta)2 dimer. Possible energy transfer pathways are discussed, briefly.
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The structure of R-phycoerythrin (R-PE) from the red alga Griffithsia monilis was solved at 1.90-A resolution by molecular replacement, using the atomic coordinates of cyanobacterial phycocyanin from Fremyella diplosiphon as a model. The crystallographic R factor for the final model is 17.5% (Rfree 22.7%) for reflections in the range 100-1.90 A. The model consists of an (alphabeta)2 dimer with an internal noncrystallographic dyad and a fragment of the gamma-polypeptide. The alpha-polypeptide (164 amino acid residues) has two covalently bound phycoerythrobilins at positions alpha82 and alpha139. The beta-polypeptide (177 residues) has two phycoerythrobilins bound to residues beta82 and beta158 and one phycourobilin covalently attached to rings A and D at residues beta50 and beta61, respectively. The electron density of the gamma-polypeptide is mostly averaged out by threefold crystallographic symmetry, but a dipeptide (Gly-Tyr) and one single Tyr could be modeled. These two tyrosine residues of the gamma-polypeptide are in close proximity to the phycoerythrobilins at position beta82 of two symmetry-related beta-polypeptides and are related by the same noncrystallographic dyad as the (alphabeta)2 dimer. Possible energy transfer pathways are discussed briefly.
==About this Structure==
==About this Structure==
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1B8D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Griffithsia_monilis Griffithsia monilis] with PEB and PUB as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B8D OCA].
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1B8D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Griffithsia_monilis Griffithsia monilis] with <scene name='pdbligand=PEB:'>PEB</scene> and <scene name='pdbligand=PUB:'>PUB</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B8D OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Diederichs, K.]]
[[Category: Diederichs, K.]]
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[[Category: Hiller, R.G.]]
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[[Category: Hiller, R G.]]
[[Category: Ritter, S.]]
[[Category: Ritter, S.]]
[[Category: Welte, W.]]
[[Category: Welte, W.]]
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[[Category: Wrench, P.M.]]
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[[Category: Wrench, P M.]]
[[Category: PEB]]
[[Category: PEB]]
[[Category: PUB]]
[[Category: PUB]]
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[[Category: red algae]]
[[Category: red algae]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:26:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:34 2008''

Revision as of 09:52, 21 February 2008


1b8d, resolution 1.90Å

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CRYSTAL STRUCTURE OF A PHYCOUROBILIN-CONTAINING PHYCOERYTHRIN

Overview

The structure of R-phycoerythrin (R-PE) from the red alga Griffithsia monilis was solved at 1.90-A resolution by molecular replacement, using the atomic coordinates of cyanobacterial phycocyanin from Fremyella diplosiphon as a model. The crystallographic R factor for the final model is 17.5% (Rfree 22.7%) for reflections in the range 100-1.90 A. The model consists of an (alphabeta)2 dimer with an internal noncrystallographic dyad and a fragment of the gamma-polypeptide. The alpha-polypeptide (164 amino acid residues) has two covalently bound phycoerythrobilins at positions alpha82 and alpha139. The beta-polypeptide (177 residues) has two phycoerythrobilins bound to residues beta82 and beta158 and one phycourobilin covalently attached to rings A and D at residues beta50 and beta61, respectively. The electron density of the gamma-polypeptide is mostly averaged out by threefold crystallographic symmetry, but a dipeptide (Gly-Tyr) and one single Tyr could be modeled. These two tyrosine residues of the gamma-polypeptide are in close proximity to the phycoerythrobilins at position beta82 of two symmetry-related beta-polypeptides and are related by the same noncrystallographic dyad as the (alphabeta)2 dimer. Possible energy transfer pathways are discussed briefly.

About this Structure

1B8D is a Protein complex structure of sequences from Griffithsia monilis with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of a phycourobilin-containing phycoerythrin at 1.90-A resolution., Ritter S, Hiller RG, Wrench PM, Welte W, Diederichs K, J Struct Biol. 1999 Jun 15;126(2):86-97. PMID:10388620

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