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1ha7

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(New page: 200px<br /><applet load="1ha7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ha7, resolution 2.20&Aring;" /> '''STRUCTURE OF A LIGHT...)
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Revision as of 14:21, 20 November 2007

Image:1ha7.gif

1ha7, resolution 2.20Å

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STRUCTURE OF A LIGHT-HARVESTING PHYCOBILIPROTEIN, C-PHYCOCYANIN FROM SPIRULINA PLATENSIS AT 2.2A RESOLUTION

Overview

The crystal structure of C-phycocyanin, a light-harvesting, phycobiliprotein from cyanobacteria (blue-green algae) Spirulina platensis, has been solved by molecular replacement technique. The crystals belong to, space group P2(1) with cell parameters a = 107.20, b = 115.40, c = 183.04, A; beta = 90.2 degrees. The structure has been refined to a, crystallographic R factor of 19.2% (R(free) = 23.9%) using the X-ray, diffraction data extending up to 2.2 A resolution. The asymmetric unit of, the crystal cell consists of two (alphabeta)6-hexamers, each hexamer being, the functional unit in the native antenna rod of cyanobacteria. The, molecular structure resembles that of other reported C-phycocyanins., However, the unique form of aggregation of two (alphabeta)6-hexamers in, the crystal asymmetric unit, suggests additional pathways of energy, transfer in lateral direction between the adjacent hexamers involving, beta155 phycocyanobilin chromophores.

About this Structure

1HA7 is a Protein complex structure of sequences from Arthrospira platensis with CYC as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of a light-harvesting protein C-phycocyanin from Spirulina platensis., Padyana AK, Bhat VB, Madyastha KM, Rajashankar KR, Ramakumar S, Biochem Biophys Res Commun. 2001 Apr 13;282(4):893-8. PMID:11352634

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