Document Detail

The 1.4 anstroms structure of dianthin 30 indicates a role of surface potential at the active site of type 1 ribosome inactivating proteins.
MedLine Citation:
PMID:  15681236     Owner:  NLM     Status:  MEDLINE    
Ribosome inactivating proteins (RIPs) are plant proteins with enzymatic activity identified as rRNA N-glycosidase (EC, which cleaves the N-glycosidic bond of a specific adenine on the ricin/sarcin region of rRNA, thus causing inhibition of protein synthesis. They also depurinate extensively DNA and other polynucleotides. The three-dimensional structure of dianthin 30, a type 1 (single-chain) RIP of Dianthus caryophyllus (leaves), is now described at 1.4 angstroms, a resolution never achieved before for any RIP. The fold typical of RIPs is conserved, despite some differences in the loop regions. The general structure comparison by superimposed alpha-carbon (249 atoms) and the sequence alignment by structure for dianthin 30 and saporin-S6 give a root mean square deviation of 0.625 angstroms. Despite the differences reported for the biological activities of the two RIPs, their structures fit quite well and both show a protein segment containing strands beta7, beta8, and beta9 shorter than other RIPs. However, the surface electrostatic potential in the active site region neatly distinguishes dianthin 30 from saporin-S6. The possible relationship between the charge distribution and the behavior of the proteins toward different substrates is discussed.
Simona Fermani; Giuseppe Falini; Alberto Ripamonti; Letizia Polito; Fiorenzo Stirpe; Andrea Bolognesi
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of structural biology     Volume:  149     ISSN:  1047-8477     ISO Abbreviation:  J. Struct. Biol.     Publication Date:  2005 Feb 
Date Detail:
Created Date:  2005-01-31     Completed Date:  2005-06-08     Revised Date:  2008-07-12    
Medline Journal Info:
Nlm Unique ID:  9011206     Medline TA:  J Struct Biol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  204-12     Citation Subset:  IM    
Dipartimento di Chimica G. Ciamician, Alma Mater Studiorum Universita' di Bologna, via Selmi 2, I-40126 Bologna, Italy.
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MeSH Terms
Amino Acid Sequence
Binding Sites
Models, Molecular
Molecular Sequence Data
Plant Proteins / chemistry,  pharmacology*
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
Protein Synthesis Inhibitors / pharmacology*
Ribosome Inactivating Proteins, Type 1
Ribosomes / drug effects*
Sequence Homology, Amino Acid
Water / chemistry
X-Ray Diffraction
Reg. No./Substance:
0/Plant Proteins; 0/Protein Synthesis Inhibitors; 0/Ribosome Inactivating Proteins, Type 1; 7732-18-5/Water

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