Crystal Structure of a Light-Harvesting Protein C-Phycocyanin from Spirulina platensis
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 P21 with cell parameters a = 107.20, b = 115.40, c = 183.04 Å; β = 90.2°. The s...
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| Veröffentlicht in: | Biochemical and Biophysical Research Communications 2001-04, Vol.282 (4), p.893-898 |
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| container_title | Biochemical and Biophysical Research Communications |
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| creator | Padyana, Anil K. Bhat, Vadiraja B. Madyastha, K.M. Rajashankar, K.R. Ramakumar, S. |
| description | 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 P21 with cell parameters a = 107.20, b = 115.40, c = 183.04 Å; β = 90.2°. The structure has been refined to a crystallographic R factor of 19.2% (Rfree = 23.9%) using the X-ray diffraction data extending up to 2.2 Å resolution. The asymmetric unit of the crystal cell consists of two (αβ)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 (αβ)6-hexamers in the crystal asymmetric unit, suggests additional pathways of energy transfer in lateral direction between the adjacent hexamers involving β155 phycocyanobilin chromophores. |
| doi_str_mv | 10.1006/bbrc.2001.4663 |
| format | Article |
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The crystals belong to space group P21 with cell parameters a = 107.20, b = 115.40, c = 183.04 Å; β = 90.2°. The structure has been refined to a crystallographic R factor of 19.2% (Rfree = 23.9%) using the X-ray diffraction data extending up to 2.2 Å resolution. The asymmetric unit of the crystal cell consists of two (αβ)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 (αβ)6-hexamers in the crystal asymmetric unit, suggests additional pathways of energy transfer in lateral direction between the adjacent hexamers involving β155 phycocyanobilin chromophores.</description><subject>bilin</subject><subject>C-Phycocyanin</subject><subject>chromophore</subject><subject>CRYSTAL STRUCTURE</subject><subject>Crystallography, X-Ray</subject><subject>Cyanobacteria - chemistry</subject><subject>Freshwater</subject><subject>light-harvesting</subject><subject>MATERIALS SCIENCE</subject><subject>Models, Molecular</subject><subject>NATIONAL SYNCHROTRON LIGHT SOURCE</subject><subject>NSLS</subject><subject>PARTICLE ACCELERATORS</subject><subject>phycobiliprotein</subject><subject>phycobiliproteins</subject><subject>Phycocyanin - chemistry</subject><subject>Protein Structure, Secondary</subject><subject>Protein Subunits</subject><subject>PROTEINS</subject><subject>Spirulina platensis</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9rFDEYhoModq29epQBobdZv_yYmeQoi9rCgoWq9BYymW-6kdlkTTKF_e-bYRc8FU_5Ak9evjcPIR8orClA-7nvo10zALoWbctfkRUFBTWjIF6TFRSiZoo-XJB3Kf0pFBWteksuKOUNa7lYkd-beEzZTNV9jrPNc8QqjJWptu5xl-sbE58wZecfq7sYMjpfbeq73dEGezS-3MYY9tX9wcV5ct5Uh8lk9Mml9-TNaKaEV-fzkvz69vXn5qbe_vh-u_myra1om1y3XCkh7MAaoSxQLoeGYVNGa9p-ZJx2CsEy4AMblUTFWA-DVdyIQfaMd_ySfDrlhrKlTtZltDsbvEebNW0ApGp4oa5P1CGGv3MppPcuWZwm4zHMSXcgGyEl_BeknZQd56yA6xNoY0gp4qgP0e1NPGoKehGjFzF6EaMXMeXBx3Py3O9x-IefTRRAngAs3_XkMC5t0FscXFzKDMG9lP0MSYubeg</recordid><startdate>20010413</startdate><enddate>20010413</enddate><creator>Padyana, Anil K.</creator><creator>Bhat, Vadiraja B.</creator><creator>Madyastha, K.M.</creator><creator>Rajashankar, K.R.</creator><creator>Ramakumar, S.</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>H99</scope><scope>L.F</scope><scope>L.G</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>20010413</creationdate><title>Crystal Structure of a Light-Harvesting Protein C-Phycocyanin from Spirulina platensis</title><author>Padyana, Anil K. ; 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The crystals belong to space group P21 with cell parameters a = 107.20, b = 115.40, c = 183.04 Å; β = 90.2°. The structure has been refined to a crystallographic R factor of 19.2% (Rfree = 23.9%) using the X-ray diffraction data extending up to 2.2 Å resolution. The asymmetric unit of the crystal cell consists of two (αβ)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 (αβ)6-hexamers in the crystal asymmetric unit, suggests additional pathways of energy transfer in lateral direction between the adjacent hexamers involving β155 phycocyanobilin chromophores.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11352634</pmid><doi>10.1006/bbrc.2001.4663</doi><tpages>6</tpages></addata></record> |
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| subjects | bilin C-Phycocyanin chromophore CRYSTAL STRUCTURE Crystallography, X-Ray Cyanobacteria - chemistry Freshwater light-harvesting MATERIALS SCIENCE Models, Molecular NATIONAL SYNCHROTRON LIGHT SOURCE NSLS PARTICLE ACCELERATORS phycobiliprotein phycobiliproteins Phycocyanin - chemistry Protein Structure, Secondary Protein Subunits PROTEINS Spirulina platensis |
| title | Crystal Structure of a Light-Harvesting Protein C-Phycocyanin from Spirulina platensis |
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