2c7l

LOW TEMPERATURE STRUCTURE OF PHYCOERYTHROCYANIN FROM MASTIGOCLADUS LAMINOSUS

spinqualitylabelsall models 2c7l, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2c7l is a 2 chain structure with sequence from Mastigocladus laminosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BLA, CYC Related: 2c7j, 2c7k Resources: FirstGlance, OCA, RCSB, PDBsum Function [PHEA_MASLA] Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. [PHEB_MASLA] Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Phycoerythrocyanin is the only cyanobacterial phycobiliprotein containing phycoviolobilin as a chromophore. The phycoviolobilin chromophore is photo-reactive; upon irradiation, the chromophore undergoes a Z/E-isomerization involving the rotation of pyrrole-ring D. We have determined the structure of trimeric phycoerythrocyanin at three different experimental settings: monochromatically at 110 K and 295 K as well as with the Laue method at 288 K. Based on their chemical structures, the restraints for the phycoviolobilin of the alpha-subunit and for the phycocyanobilin chromophores of the beta-subunit were newly generated, which allows a chemically meaningful refinement of both chromophores. All three phycoerythrocyanin structures are very similar; the subunits match within 0.5 A. The detailed comparison of the data obtained with the different measurements provided information about the protein properties around the phycoviolobilin chromophore. For the first time, crystals of a phycobilisome protein are used successfully with the Laue technique. This paves the way for time-resolved macromolecular crystallography, which is able to elucidate the exact mechanisms of the phycoviolobilin photoactivity including the protein involvement. Local protein flexibility as a prerequisite for reversible chromophore isomerization in alpha-phycoerythrocyanin.,Schmidt M, Krasselt A, Reuter W Biochim Biophys Acta. 2006 Jan;1764(1):55-62. Epub 2005 Nov 21. PMID:16377266 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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