3v58 | pdb_00003v58

Crystal Structure of the B-phycoerythrin from the red algae Porphyridium Cruentum at pH5

spinqualitylabelsall models 3v58, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3v58 is a 4 chain structure with sequence from Porphyridium purpureum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PEB, SO4 NonStd Res: MEN Related: 3v57 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed B-phycoerythrin from the red alga Porphyridium cruentum was crystallized using the technique of capillary counter-diffusion. Crystals belonging to the space group R3 with almost identical unit cell constants and diffracting to 1.85 and 1.70 A were obtained at pH values of 5 and 8, respectively. The most important difference between structures is the presence of the residue His88alpha in two different conformations at pH 8. This residue is placed next to the chromophore phycoerythrobilin PEB82alpha and the new conformation results in the relocation of the hydrogen-bond network and hydration around PEB82alpha, which probably contributes to the observed pH dependence of the optical spectrum associated with this chromophore. Comparison with the structures of B-phycoerythrin from other red algae shows differences in the conformation of the A-ring of the chromophore PEB139alpha. This conformational difference in B-phycoerythrin from P. cruentum enables the formation of several hydrogen bonds that connect PEB139alpha with the chromophore PEB158beta at the (alphabeta)(3) hexamer association interface. The possible influence of these structural differences on the optical spectrum and the ability of the protein to perform energy transfer are discussed, with the two pH-dependent conformations of His88alpha and PEB82alpha being proposed as representing critical structural features that are correlated with the pH dependence of the optical spectrum and transient optical states during energy transfer. DATABASE: Structural data have been deposited in the Protein Data Bank under accession numbers 3V58 and 3V57. STRUCTURED DIGITAL ABSTRACT: B-phycoerythrin beta and B-phycoerythrin alpha bind by x-ray crystallography (View interaction). pH-dependent structural conformations of B-phycoerythrin from Porphyridium cruentum.,Camara-Artigas A, Bacarizo J, Andujar-Sanchez M, Ortiz-Salmeron E, Mesa-Valle C, Cuadri C, Martin-Garcia JM, Martinez-Rodriguez S, Mazzuca-Sobczuk T, Ibanez MJ, Allen JP FEBS J. 2012 Oct;279(19):3680-91. doi: 10.1111/j.1742-4658.2012.08730.x. Epub, 2012 Sep 4. PMID:22863205 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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