5tou

STRUCTURE OF C-PHYCOCYANIN FROM ARCTIC PSEUDANABAENA SP. LW0831

spinqualitylabelsall models 5tou, resolution 2.04Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5tou is a 12 chain structure with sequence from Pseudanabaena sp. lw0831. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.04Å Ligands: CYC, MEN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function V5NXI0_9CYAN Publication Abstract from PubMed The cold adaptation mechanism of phycobiliproteins, the major photosynthetic pigment-proteins in cyanobacteria and red algae, has rarely been studied. Here we reported the biochemical, structural, and molecular dynamics simulation study of the C-phycocyanin from Arctic cyanobacterial strain Pseudanabaena sp. LW0831. We characterized the phycobilisome components of LW0831 and obtained their gene sequences. Compared to the mesophilic counterpart from Arthrospira platensis (Ar-C-PC), LW0831 C-phycocyanin (Ps-C-PC) has a decreased thermostability (Tm of -16 degrees C), one of the typical features of cold-adapted enzymes. To uncover its structural basis, we resolved the crystal structure of Ps-C-PC 1 at 2.04A. Consistent with the decrease in thermostability, comparative structural analyses revealed decreased intra-trimer and inter-trimer interactions in Ps-C-PC 1, compared to Ar-C-PC. However, comparative molecular dynamics simulations indicated that Ps-C-PC 1 shows similar flexibilities to Ar-C-PC for both the (alphabeta)3 trimer and (alphabeta)6 hexamer. Therefore, the optimization mode is clearly different from cold-adapted enzymes, which usually have increased flexibilities. Detailed analyses demonstrated different optimization modes for the alpha and beta subunits and it was revealed that hydrophobic interactions are key to this difference, though salt bridges, hydrogen bonds, and surface hydrophobicity are also involved. This study is the first report of the structure of cold-adapted phycobiliproteins and provides insights into the cold-adaptation strategies of non-enzyme proteins. Structural insights into the cold adaptation of the photosynthetic pigment-protein C-phycocyanin from an Arctic cyanobacterium.,Su HN, Wang QM, Li CY, Li K, Luo W, Chen B, Zhang XY, Qin QL, Zhou BC, Chen XL, Zhang YZ, Xie BB Biochim Biophys Acta. 2017 Apr;1858(4):325-335. doi:, 10.1016/j.bbabio.2017.02.004. Epub 2017 Feb 7. PMID:28188780 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phycocyanin

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