4rmp | pdb_00004rmp

Crystal structure of allophycocyanin from marine cyanobacterium Phormidium sp. A09DM

spinqualitylabelsall models 4rmp, resolution 2.51Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4rmp is a 2 chain structure with sequence from Phormidium rubidum A09DM. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.506Å Ligands: CYC, MEN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A078K1U6_9CYAN Publication Abstract from PubMed Isolated phycobilisome (PBS) sub-assemblies have been widely subjected to X-ray crystallography analysis to obtain greater insights into the structure-function relationship of this light harvesting complex. Allophycocyanin (APC) is the phycobiliprotein always found in the PBS core complex. Phycocyanobilin (PCB) chromophores, covalently bound to conserved Cys residues of alpha- and beta- subunits of APC, are responsible for solar energy absorption from phycocyanin and for transfer to photosynthetic apparatus. In the known APC structures, heterodimers of alpha- and beta- subunits (known as alphabeta monomers) assemble as trimer or hexamer. We here for the first time report the crystal structure of APC isolated from a marine cyanobacterium (Phormidium sp. A09DM). The crystal structure has been refined against all the observed data to the resolution of 2.51 A to Rwork (Rfree) of 0.158 (0.229) with good stereochemistry of the atomic model. The Phormidium protein exists as a trimer of alphabeta monomers in solution and in crystal lattice. The overall tertiary structures of alpha- and beta- subunits, and trimeric quaternary fold of the Phormidium protein resemble the other known APC structures. Also, configuration and conformation of the two covalently bound PCB chromophores in the marine APC are same as those observed in fresh water cyanobacteria and marine red algae. More hydrophobic residues, however, constitute the environment of the chromophore bound to alpha-subunit of the Phormidium protein, owing mainly to amino acid substitutions in the marine protein. Crystal Structure of Allophycocyanin from Marine Cyanobacterium Phormidium sp. A09DM.,Sonani RR, Gupta GD, Madamwar D, Kumar V PLoS One. 2015 Apr 29;10(4):e0124580. doi: 10.1371/journal.pone.0124580., eCollection 2015. PMID:25923120 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Allophycocyanin 3D structures

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