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The three‐dimensional structure of “Lonely Guy” from C laviceps purpurea provides insights into the phosphoribohydrolase function of R ossmann fold‐containing lysine decarboxylase‐like proteins
Author(s) -
Dzurová Lenka,
Forneris Federico,
Savino Simone,
Galuszka Petr,
Vrabka Josef,
Frébort Ivo
Publication year - 2015
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24835
Subject(s) - enzyme , lysine , nucleotide , biochemistry , stereochemistry , monomer , homology (biology) , biology , function (biology) , chemistry , amino acid , genetics , gene , organic chemistry , polymer
The recently discovered cytokinin (CK)‐specific phosphoribohydrolase “Lonely Guy” (LOG) is a key enzyme of CK biosynthesis, converting inactive CK nucleotides into biologically active free bases. We have determined the crystal structures of LOG from Claviceps 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. Proteins 2015; 83:1539–1546. © 2015 Wiley Periodicals, Inc.