2x20 | pdb_00002x20

Structure of Peridinin-Chlorophyll-Protein reconstituted with Chl-b

spinqualitylabelsall models 2x20, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2x20 is a 1 chain structure with sequence from Amphidinium carterae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Ligands: CD, CL, DGD, K, NA, PEG, PID Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PCP1_AMPCA Water-soluble antenna for capture of solar energy in the blue-green range. Peridinin is an asymmetric carotenoid. 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 The peridinin-chlorophyll a-protein (PCP) from dinoflagellates is a soluble light harvesting antenna which gathers incoming photons mainly by the carotenoid peridinin. In PCPs reconstituted with different chlorophylls, the peridinin to chlorophyll energy transfer rates are well predicted by a Forster-like theory, but only if the pigment arrangements are identical in all PCPs. We have determined the X-ray structures of PCPs reconstituted with Chlorophyll-b (Chl-b), Chlorophyll-d (Chl-d) and Bacteriochlorophyll-a (BChl-a) to resolutions<or=2A. In all three cases the pigment arrangements are essentially the same as in native PCP. Hydrogen bonding is not responsible for preferential incorporation of "non-native" chlorophylls over Chl-a. X-ray structures of the peridinin-chlorophyll-protein reconstituted with different chlorophylls.,Schulte T, Hiller RG, Hofmann E FEBS Lett. 2010 Mar 5;584(5):973-8. Epub 2010 Jan 25. PMID:20102711 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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