1gh0

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(New page: 200px<br /><applet load="1gh0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gh0, resolution 2.2&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1gh0.gif|left|200px]]<br /><applet load="1gh0" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1gh0, resolution 2.2&Aring;" />
caption="1gh0, resolution 2.2&Aring;" />
'''CRYSTAL STRUCTURE OF C-PHYCOCYANIN FROM SPIRULINA PLATENSIS'''<br />
'''CRYSTAL STRUCTURE OF C-PHYCOCYANIN FROM SPIRULINA PLATENSIS'''<br />
==Overview==
==Overview==
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The crystal structure of C-phycocyanin from the cyanobacterium S., platensis has been determined at 2.2 A resolution. The crystals belong to, the monoclinic crystal form, which has not been previously reported for, phycobiliprotein structures. The structure was solved using the, molecular-replacement method with a final R value of 18.9% (R(free) =, 23.7%) after model building and refinement. In the crystals used for the, study, the C-phycocyanin hexamers formed by face-to-face association of, two trimers are arranged in layers rather than in columns. Three different, kinds of packing between adjacent hexamers in the layer were compared. The, tight packing of two adjacent hexamers formed by four trimers in the, asymmetric unit brings beta155 PCB chromophores close together, so it is, possible that lateral energy transfer takes place through the, beta155-beta155 route.
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The crystal structure of C-phycocyanin from the cyanobacterium S. platensis has been determined at 2.2 A resolution. The crystals belong to the monoclinic crystal form, which has not been previously reported for phycobiliprotein structures. The structure was solved using the molecular-replacement method with a final R value of 18.9% (R(free) = 23.7%) after model building and refinement. In the crystals used for the study, the C-phycocyanin hexamers formed by face-to-face association of two trimers are arranged in layers rather than in columns. Three different kinds of packing between adjacent hexamers in the layer were compared. The tight packing of two adjacent hexamers formed by four trimers in the asymmetric unit brings beta155 PCB chromophores close together, so it is possible that lateral energy transfer takes place through the beta155-beta155 route.
==About this Structure==
==About this Structure==
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1GH0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Arthrospira_platensis Arthrospira platensis] with CYC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GH0 OCA].
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1GH0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Arthrospira_platensis Arthrospira platensis] with <scene name='pdbligand=CYC:'>CYC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GH0 OCA].
==Reference==
==Reference==
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[[Category: Arthrospira platensis]]
[[Category: Arthrospira platensis]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Chang, W.R.]]
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[[Category: Chang, W R.]]
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[[Category: Liang, D.C.]]
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[[Category: Liang, D C.]]
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[[Category: Wang, X.Q.]]
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[[Category: Wang, X Q.]]
[[Category: CYC]]
[[Category: CYC]]
[[Category: c-phycocyanin from spirulina platensis]]
[[Category: c-phycocyanin from spirulina platensis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:03:01 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:50:02 2008''

Revision as of 10:50, 21 February 2008


1gh0, resolution 2.2Å

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CRYSTAL STRUCTURE OF C-PHYCOCYANIN FROM SPIRULINA PLATENSIS

Overview

The crystal structure of C-phycocyanin from the cyanobacterium S. platensis has been determined at 2.2 A resolution. The crystals belong to the monoclinic crystal form, which has not been previously reported for phycobiliprotein structures. The structure was solved using the molecular-replacement method with a final R value of 18.9% (R(free) = 23.7%) after model building and refinement. In the crystals used for the study, the C-phycocyanin hexamers formed by face-to-face association of two trimers are arranged in layers rather than in columns. Three different kinds of packing between adjacent hexamers in the layer were compared. The tight packing of two adjacent hexamers formed by four trimers in the asymmetric unit brings beta155 PCB chromophores close together, so it is possible that lateral energy transfer takes place through the beta155-beta155 route.

About this Structure

1GH0 is a Protein complex structure of sequences from Arthrospira platensis with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of C-phycocyanin from Spirulina platensis at 2.2 A resolution: a novel monoclinic crystal form for phycobiliproteins in phycobilisomes., Wang XQ, Li LN, Chang WR, Zhang JP, Gui LL, Guo BJ, Liang DC, Acta Crystallogr D Biol Crystallogr. 2001 Jun;57(Pt 6):784-92. Epub 2001, May 25. PMID:11375497

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