Dashed lines (black) labeled with numbers in Å represent hydrogen bonds. 1995 Jul 14;250(3):354-67. doi: 10.1006/jmbi.1995.0382.Collins EJ, Robertus JD, LoPresti M, Stone KL, Williams KR, Wu P, Hwang K, Piatak M.Lin SH, Chow LP, Chen YL, Liaw YC, Chen JK, Lin JY.Eur J Biochem. Abrin can be extracted from jequirity beans using a relatively simple and cheap procedure. Amino acid residues (green/cyan) and bound ligands (yellow/gray) are shown in a stick model. 1996 Sep 15;240(3):564-9. doi: 10.1111/j.1432-1033.1996.0564h.x.J Biomed Sci. Comparison of the amino acid sequence of abrin-a B chain with that of ricin-D B chain reveals a high degree of sequence identity (59%). In terms of structure, abrin-a is related to the lectin, ricin, produced in the seeds of Ricinus communis. Surface of protein (smudge/slate) is drawn to illustrate the active site cleft. The B chain is a galactose-specific lectin that facilitates the binding of abrin to the cell membrane that precedes endocytosis. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes,Single‐chain ribosome inactivating proteins from plants depurinate,Pokeweed antiviral protein: ribosome inactivation and therapeutic applications,Ribosome‐inactivating proteins: progress and problems,Differences in ribosome binding and Sarcin/Ricin loop depurination by Shiga and Ricin holotoxins,Analysis of several key active site residues of ricin A chain by mutagenesis and X‐ray crystallography,Site‐directed mutagenesis of ricin A‐chain and implications for the mechanism of action,X‐ray analysis of substrate analogs in the ricin A‐chain active site,Transition state analogues in structures of ricin and saporin ribosome‐inactivating proteins,Ricin A‐chain: kinetics, mechanism, and RNA stem‐loop inhibitors,Ricin A‐Chain: Kinetic isotope effects and transition state structure with stem‐loop RNA,Transition state structure of RNA depurination by saporin L3,Studies on crystal structures, active‐centre geometry and depurinating mechanism of two ribosome‐inactivating proteins,Crystal structures of the complexes of trichosanthin with four substrate analogs and catalytic mechanism of RNA N‐glycosidase,Substrate binding and catalysis in trichosanthin occur in different sites as revealed by the complex structures of several E85 mutants,The N‐glycosidase mechanism of ribosome‐inactivating proteins implied by crystal structures of alpha momorcharin,Biological and chemical terrorism: strategic plan for preparedness and response. The,Identification of catalytic water implicated in the hydrolysis of N‐glycosidic bond of susceptible adenosine at ABA active site. The reaction mixture was incubated for 1 h at 37 °C and the protein synthesis was monitored by the luminescence obtained by the addition of the luciferin substrate. 2010 Apr 30;17(1):34. doi: 10.1186/1423-0127-17-34.Biochem J. (A) Cartoon representation of generated ABA‐SRL model indicating binding of invariant GA,Schematic diagram of interactions observed in the ABA‐SRL model.
and you may need to create a new Wiley Online Library account.Enter your email address below and we will send you your username,If the address matches an existing account you will receive an email with instructions to retrieve your username,Overview of ABA structure and its active site geometry pre and post N‐glycosidase activity. The sequence is not identical with that predicted previously by nucleotide sequencing, indicating the presence of isoforms of abrin. Amino acid residues (green) and ligands (yellow/white) are shown in a stick model. Distances are shown as dashed lines (magenta/black) labeled with numbers in Å. The,Emergence of two pockets at ABA active site cleft upon substrate binding. The polymer mastic composition represents a suspension of fillers of modifying additives, stabilizers and synthetic rubbers in … In (A) and (B), the two pockets at ABA (smudge) active site cleft, separated by active site Y74, are shown in ABA‐Adenine and ABA‐Nicotinamide structures.
Please enable it to take advantage of the complete set of features!Clipboard, Search History, and several other advanced features are temporarily unavailable.National Center for Biotechnology Information,Unable to load your collection due to an error,Unable to load your delegates due to an error.Biosci Biotechnol Biochem. This figure was generated using NUCPLOT,Comparison of ABA‐SRL interface in rigid‐body docked and flexibly docked ABA‐SRL model. Abrin is a toxic protein obtained from the seeds of Abrus precatorius (jequirity bean), which is similar in structure and properties to ricin. The sequence is not identical with that predicted previously by … Nitrogen, oxygen, and phosphorus atoms are colored blue, red, and orange, respectively while carbon atoms are colored according to the color mentioned for residues or ligands. (C) The absence of two pocket feature in apo‐ABA structure is indicated. Protein and RNA residues are shown in a stick model. The crystal structure of abrin-a, a type II ribosome-inactivating protein from the seeds of Abrus precatorius, has been determined from a novel crystalline form by the molecular replacement method using the coordinates of ricin.
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