The three-dimensional structure of "Lonely Guy" from Claviceps purpurea provides insights into the phosphoribohydrolase function of Rossmann fold-containing lysine decarboxylase-like proteins
Jazyk angličtina Země Spojené státy americké Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
26010010
DOI
10.1002/prot.24835
Knihovny.cz E-zdroje
- Klíčová slova
- Claviceps purpurea, Rossmann fold, cytokinin, lysine decarboxylase, phosphoribohydrolase, protein lonely guy,
- MeSH
- aminohydrolasy chemie metabolismus MeSH
- Claviceps enzymologie MeSH
- cytokininy metabolismus MeSH
- fungální proteiny chemie metabolismus MeSH
- karboxylyasy chemie metabolismus MeSH
- molekulární modely * MeSH
- sekvence aminokyselin MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- aminohydrolasy MeSH
- cytokininy MeSH
- fungální proteiny MeSH
- karboxylyasy MeSH
- lysine decarboxylase MeSH Prohlížeč
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.
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