Crystal structure of PD-L1, a ribosome inactivating protein from Phytolacca dioica L. leaves with the property to induce DNA cleavage
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Crystal structure of PD-L1, a ribosome inactivating protein from Phytolacca dioica L. leaves with the property to induce DNA cleavage (127 visite)

Ruggiero A, Di Maro A, Severino V, Chambery A, Berisio R

Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2009 Dec; 91(12): 1135-1142.



Tipo di articolo: Journal Article,

Impact factor: 2.605, Impact factor a 5 anni: 2.474

Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-71749090850&partnerID=40&md5=6abbd805dd16f63a0563471ce03a0feb

Parole chiave: Crystal, Dna, Ribosome Inactivating Protein, Dna Cleavage, Double Strands, E. Coli, Functional Behaviors, Functional Changes, Glycosylated, Molecular Replacements, Phase Determination, Plasmid Pbr322, Ribosome-Inactivating Protein, Seeding Techniques, Structural Determinants, Two-Component, Escherichia Coli, Esterification, Fluorine Containing Polymers, Genes, Glycosylation, Nucleic Acids, Single Crystals, X Ray Crystallography, Crystal Structure, Protein Pd L1, Unclassified Drug, Vegetable Protein, Double Stranded Dna, Amino Acid Sequence, Article, Controlled Study, Nonhuman, Plant Leaf, Pokeweed, Protein Dna Interaction, Protein Expression, Protein Family, Protein Function, Protein Glycosylation, Protein Structure, Sequence Analysis, Binding Sites, X-Ray, Bacterial, Models, Molecular Sequence Data, Phytolacca, Plant Leaves, Plant Proteins, Protein Isoforms, Secondary, Tertiary, Recombinant Proteins, Type 1, Sequence Homology, Phytolacca Dioica,

Affiliazioni:

*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini, C.N.R., Napoli I-80134, Italy
Dipartimento di Scienze Della Vita, Seconda Università di Napoli, Via Vivaldi 43, Caserta I-81100, Italy


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The structure of the highly glycosylated type 1 ribosome inactivating protein PD-L1 was determined by X-ray crystallography. This protein belongs to a group of four PD-Ls (PD-L1-4) expressed in Phytolacca dioica leaves. Of these, PD-L1 and PD-L2 are endowed with the ability to cleave double strand DNA, a property which is not shared by the other two components of the family. Single crystals of native PD-L1, the most glycosylated, were obtained using seeding techniques and phase determination was achieved using molecular replacement. To investigate the role of glycosylation in the different functionality of these proteins, we performed DNA cleavage assays on the E. coli plasmid pBR322. These experiments revealed that DNA cleaving ability does not depend on the level of glycosylation of PD-L1, since there is no difference in the activities displayed by native PD-L1 and a recombinant non-glycosylated form. Besides, confirming that DNA cleavage by PD-L1 cannot be attributed to contaminations, these data unambiguously show that functional changes between PD-L1 and PD-L4 are solely to be attributed to their sequence differences. On the basis of the comparison of PD-L1 and PD-L4 crystal structures, we propose possible structural determinants responsible for their different functional behavior. © 2009 Wiley Periodicals, Inc.
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