4lmx

Light harvesting complex PE555 from the cryptophyte Hemiselmis andersenii CCMP644

spinqualitylabelsall models 4lmx, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4lmx is a 12 chain structure with sequence from Hemiselmis andersenii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: DBV, LYZ, PEB Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PHEA2_HEMAN Light-harvesting photosynthetic tetrapyrrole chromophore-protein from the phycobiliprotein complex. Publication Abstract from PubMed Observation of coherent oscillations in the 2D electronic spectra (2D ES) of photosynthetic proteins has led researchers to ask whether nontrivial quantum phenomena are biologically significant. Coherent oscillations have been reported for the soluble light-harvesting phycobiliprotein (PBP) antenna isolated from cryptophyte algae. To probe the link between spectral properties and protein structure, we determined crystal structures of three PBP light-harvesting complexes isolated from different species. Each PBP is a dimer of alphabeta subunits in which the structure of the alphabeta monomer is conserved. However, we discovered two dramatically distinct quaternary conformations, one of which is specific to the genus Hemiselmis. Because of steric effects emerging from the insertion of a single amino acid, the two alphabeta monomers are rotated by approximately 73 degrees to an "open" configuration in contrast to the "closed" configuration of other cryptophyte PBPs. This structural change is significant for the light-harvesting function because it disrupts the strong excitonic coupling between two central chromophores in the closed form. The 2D ES show marked cross-peak oscillations assigned to electronic and vibrational coherences in the closed-form PC645. However, such features appear to be reduced, or perhaps absent, in the open structures. Thus cryptophytes have evolved a structural switch controlled by an amino acid insertion to modulate excitonic interactions and therefore the mechanisms used for light harvesting. Single-residue insertion switches the quaternary structure and exciton states of cryptophyte light-harvesting proteins.,Harrop SJ, Wilk KE, Dinshaw R, Collini E, Mirkovic T, Teng CY, Oblinsky DG, Green BR, Hoef-Emden K, Hiller RG, Scholes GD, Curmi PM Proc Natl Acad Sci U S A. 2014 Jul 1;111(26):E2666-75. doi:, 10.1073/pnas.1402538111. Epub 2014 Jun 16. PMID:24979784 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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