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5aju

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Crystal structure of ligand-free phosphoribohydroxylase lonely guy from Claviceps purpurea in complex with phosphoribose

Structural highlights

5aju is a 1 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 2.5Å
Ligands:	,
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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Dzurova L, Forneris F, Savino S, Galuszka P, Vrabka J, Frebort I. The three-dimensional Structure of "Lonely Guy" from Claviceps purpurea provides insights into the phosphoribohydrolase function of Rossmann fold-containing lysine decarboxylase-like proteins. Proteins. 2015 May 25. doi: 10.1002/prot.24835. PMID:26010010 doi:http://dx.doi.org/10.1002/prot.24835