1m98 | pdb_00001m98

Crystal Structure of Orange Carotenoid Protein

spinqualitylabelsall models 1m98, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1m98 is a 2 chain structure with sequence from Arthrospira maxima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, HEQ, SUC Resources: FirstGlance, OCA, RCSB, PDBsum 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 Carotenoids undergo a wide range of photochemical reactions in animal, plant, and microbial systems. In photosynthetic organisms, in addition to light harvesting, they perform an essential role in protecting against light-induced damage by quenching singlet oxygen, superoxide anion radicals, or triplet-state chlorophyll. We have determined the crystal structure of a water-soluble orange carotenoid protein (OCP) isolated from the cyanobacterium Arthrospira maxima at a resolution of 2.1 A. OCP forms a homodimer with one carotenoid molecule per monomer. The carotenoid binding site is lined by a striking number of methionine residues. The structure reveals several possible ways in which the protein environment influences the spectral properties of the pigment and provides insight into how the OCP carries out its putative functions in photoprotection. The crystal structure of a cyanobacterial water-soluble carotenoid binding protein.,Kerfeld CA, Sawaya MR, Brahmandam V, Cascio D, Ho KK, Trevithick-Sutton CC, Krogmann DW, Yeates TO Structure. 2003 Jan;11(1):55-65. PMID:12517340 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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