3le7

Crystal structure of PD-L1 from P. dioica in complex with adenine

spinqualitylabelsall models 3le7, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3le7 is a 2 chain structure with sequence from Phytolacca dioica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADE, NAG Related: 3h5k Activity: rRNA N-glycosylase, with EC number 3.2.2.22 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RIPL1_PHYDI] Inhibits protein synthesis. Cleaves supercoiled pBR322 dsDNA. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed N-glycosylation is one of the major naturally occurring covalent co-translational modifications of proteins in plants, being involved in proteins structure, folding, stability and biological activity. In the present work the influence of carbohydrate moieties on the structure-function relationships of type 1 ribosome-inactivating proteins (RIPs) was investigated. To this aim, PD-Ls, RIPs isolated from Phytolacca dioica L. leaves, differing for their glycosylation degree, were used as an experimental system. In particular, comparative structural and biological analyses were performed using native and unglycosylated recombinant PD-L1, the most glycosylated P. dioica RIP isoform. The glycans influence on protein synthesis inhibition and adenine polynucleotide glycosidase activity was investigated. The interaction with adenine, the product of the de-adenylation reaction, was also investigated for native and recombinant PD-L1 by fluorescence spectroscopy. Furthermore, the crystal structure of PD-L1 in complex with adenine was determined. Our data confirm that the absence of glycan moieties did not affect the biological activity in terms of protein synthesis inhibition. However, the removal of carbohydrate chains significantly increased the deadenylation capability, likely as a consequence of the increased accessibility of substrates to the active site pocket. Furthermore, preliminary data on cellular uptake showed that all PD-L isoforms were internalized and, for the first time, that the vesicular distribution within cells could be influenced by the protein glycosylation degree. The role of the glycan moiety on the structure-function relationships of PD-L1, type 1 ribosome-inactivating protein from P. dioica leaves.,Severino V, Chambery A, Di Maro A, Marasco D, Ruggiero A, Berisio R, Giansanti F, Ippoliti R, Parente A Mol Biosyst. 2010 Mar;6(3):570-9. Epub 2010 Jan 21. PMID:20174685 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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