The three-dimensional structure of "Lonely Guy" from Claviceps purpurea provides insights into the phosphoribohydrolase function of Rossmann fold-containing lysine decarboxylase-like proteins
Language English Country United States Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
26010010
DOI
10.1002/prot.24835
Knihovny.cz E-resources
- Keywords
- Claviceps purpurea, Rossmann fold, cytokinin, lysine decarboxylase, phosphoribohydrolase, protein lonely guy,
- MeSH
- Aminohydrolases chemistry metabolism MeSH
- Claviceps enzymology MeSH
- Cytokinins metabolism MeSH
- Fungal Proteins chemistry metabolism MeSH
- Carboxy-Lyases chemistry metabolism MeSH
- Models, Molecular * MeSH
- Amino Acid Sequence MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Aminohydrolases MeSH
- Cytokinins MeSH
- Fungal Proteins MeSH
- Carboxy-Lyases MeSH
- lysine decarboxylase MeSH Browser
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.
References provided by Crossref.org
Biochemical and Structural Aspects of Cytokinin Biosynthesis and Degradation in Bacteria
