5y42 | pdb_00005y42
Native-crystal structure of three chain non-toxic type II ribosome inactivating protein purified from the seeds of Trichosanthes anguina
Structural highlights
Function[SGSL_TRIAN] Seed lectin similar to type 2 ribosome-inactivating proteins (PubMed:23897472, PubMed:11375527). The Aalpha and Abeta chains constitute the rRNA glycosidase domain and the B chain the carbohydrate-binding lectin domain (PubMed:23897472). Is predicted to have no glycosidase activity and, hence, to be non-toxic, due to small changes in both the nucleotide binding and carbohydrate binding capabilities (PubMed:23897472, PubMed:11375527). Binds galactose and derivatives with a preference for the beta-anomeric forms (PubMed:8799450, PubMed:10877067). Binds prophyrins (PubMed:10877067). Has hemagglutinating activity towards rabbit and human erythrocytes (PubMed:8799450, PubMed:10877067).[1] [2] [3] [4] Publication Abstract from PubMedThe sequence and structure of snake gourd seed lectin (SGSL), a nontoxic homologue of type II ribosome-inactivating proteins (RIPs), have been determined by mass spectrometry and X-ray crystallography, respectively. As in type II RIPs, the molecule consists of a lectin chain made up of two beta-trefoil domains. The catalytic chain, which is connected through a disulfide bridge to the lectin chain in type II RIPs, is cleaved into two in SGSL. However, the integrity of the three-dimensional structure of the catalytic component of the molecule is preserved. This is the first time that a three-chain RIP or RIP homologue has been observed. A thorough examination of the sequence and structure of the protein and of its interactions with the bound methyl-alpha-galactose indicate that the nontoxicity of SGSL results from a combination of changes in the catalytic and the carbohydrate-binding sites. Detailed analyses of the sequences of type II RIPs of known structure and their homologues with unknown structure provide valuable insights into the evolution of this class of proteins. They also indicate some variability in carbohydrate-binding sites, which appears to contribute to the different levels of toxicity exhibited by lectins from various sources. The sequence and structure of snake gourd (Trichosanthes anguina) seed lectin, a three-chain nontoxic homologue of type II RIPs.,Sharma A, Pohlentz G, Bobbili KB, Jeyaprakash AA, Chandran T, Mormann M, Swamy MJ, Vijayan M Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1493-503. doi:, 10.1107/S0907444913010020. Epub 2013 Jul 18. PMID:23897472[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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