5AJT
Crystal structure of ligand-free phosphoribohydrolase lonely guy from Claviceps purpurea
Summary for 5AJT
| Entry DOI | 10.2210/pdb5ajt/pdb |
| Related | 5AJU |
| Descriptor | PHOSPHORIBOHYDROLASE LONELY GUY, 1,2-ETHANEDIOL, D(-)-TARTARIC ACID, ... (4 entities in total) |
| Functional Keywords | hydrolase, cytokinin, rossmann fold, lysine decarboxylase |
| Biological source | CLAVICEPS PURPUREA (ERGOT FUNGUS) |
| Total number of polymer chains | 4 |
| Total formula weight | 117748.50 |
| Authors | Dzurova, L.,Savino, S.,Forneris, F. (deposition date: 2015-02-27, release date: 2015-06-03, Last modification date: 2024-01-10) |
| Primary citation | 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, 83:1539-1546, 2015 Cited by PubMed Abstract: 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. PubMed: 26010010DOI: 10.1002/prot.24835 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.43 Å) |
Structure validation
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