4f0t | pdb_00004f0t

X-Ray Crystal Structure of Phycocyanin from Synechocystis sp. PCC 6803

spinqualitylabelsall models 4f0t, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4f0t is a 2 chain structure with sequence from Synechocystis sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CYC NonStd Res: MEN Related: 4f0u, 1on7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PHCA_SYNY3] Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. [PHCB_SYNY3] Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex. Publication Abstract from PubMed X-ray crystal structures of the isolated phycobiliprotein components of the phycobilisome have provided high resolution details to the description of this light harvesting complex at different levels of complexity and detail. The linker-independent assembly of trimers into hexamers in crystal lattices of previously determined structures has been observed in almost all of the phycocyanin (PC) and allophycocyanin (APC) structures available in the Protein Data Bank. In this paper we describe the X-ray crystal structures of PC and APC from Synechococcus elongatus sp. PCC 7942, PC from Synechocystis sp. PCC 6803 and PC from Thermosynechococcus vulcanus crystallized in the presence of urea. All five structures are highly similar to other PC and APC structures on the levels of subunits, monomers and trimers. The Synechococcus APC forms a unique loose hexamer that may show the structural requirements for core assembly and rod attachment. While the Synechococcus PC assembles into the canonical hexamer, it does not further assemble into rods. Unlike most PC structures, the Synechocystis PC fails to form hexamers. Addition of low concentrations of urea to T. vulcanus PC inhibits this proteins propensity to form hexamers, resulting in a crystal lattice composed of trimers. The molecular source of these differences in assembly and their relevance to the phycobilisome structure is discussed. Allophycocyanin and phycocyanin crystal structures reveal facets of phycobilisome assembly.,Marx A, Adir N Biochim Biophys Acta. 2013 Mar;1827(3):311-8. doi: 10.1016/j.bbabio.2012.11.006. , Epub 2012 Nov 28. PMID:23201474 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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