5ajt

Crystal structure of ligand-free phosphoribohydrolase lonely guy from Claviceps purpurea

spinqualitylabelsall models 5ajt, resolution 2.43Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ajt is a 4 chain structure with sequence from Claviceps purpurea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.43Å Ligands: EDO, TAR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function M1VUY5_CLAP2 Publication Abstract from PubMed The recently discovered cytokinin-specific phosphoribohydrolase 'Lonely Guy' (LOG) is a key enzyme of cytokinin biosynthesis, converting inactive cytokinin nucleotides into biologically active free-bases. We have determined the crystal structures of LOG from C. purpurea (cpLOG) and its complex with the enzymatic product phosphoribose. The structures reveal a dimeric arrangement of Rossmann folds, with the ligands bound to large pockets at the interface between cpLOG monomers. Structural comparisons highlight the homology of cpLOG to putative lysine decarboxylases. Extended sequence analysis enabled identification of a distinguishing LOG sequence signature. Taken together, our data suggest phosphoribohydrolase activity for several proteins of unknown function. This article is protected by copyright. All rights reserved. The three-dimensional Structure of "Lonely Guy" from Claviceps purpurea provides insights into the phosphoribohydrolase function of Rossmann fold-containing lysine decarboxylase-like proteins.,Dzurova L, Forneris F, Savino S, Galuszka P, Vrabka J, Frebort I Proteins. 2015 May 25. doi: 10.1002/prot.24835. PMID:26010010 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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