1pc8
From Proteopedia
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'''Crystal Structure of a novel form of mistletoe lectin from Himalayan Viscum album L. at 3.8A resolution''' | '''Crystal Structure of a novel form of mistletoe lectin from Himalayan Viscum album L. at 3.8A resolution''' | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Viscum album]] | [[Category: Viscum album]] | ||
| - | [[Category: | + | [[Category: RRNA N-glycosylase]] |
[[Category: Babu, C R.]] | [[Category: Babu, C R.]] | ||
[[Category: Ethayathulla, A S.]] | [[Category: Ethayathulla, A S.]] | ||
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[[Category: Singh, T P.]] | [[Category: Singh, T P.]] | ||
[[Category: Yadav, S.]] | [[Category: Yadav, S.]] | ||
| - | [[Category: | + | [[Category: Crystal structure]] |
| - | [[Category: | + | [[Category: Mistletoe lectin]] |
| - | [[Category: | + | [[Category: Novel form]] |
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Revision as of 01:55, 3 May 2008
Crystal Structure of a novel form of mistletoe lectin from Himalayan Viscum album L. at 3.8A resolution
Overview
This is the first report of the structural studies of a novel ribosome-inactivating protein (RIP) obtained from the Himalayan mistletoe (Viscum album) (HmRip). HmRip is a type II heterodimeric protein consisting of a toxic enzyme (A-chain) with an active site for ribosome inactivation and a lectin subunit (B-chain) with well defined sugar-binding sites. The crystal structure of HmRip has been determined at 3.8 A resolution and refined to a crystallographic R factor of 0.228 (R(free) = 0.271). A comparison of this structure with other type II RIPs reveals the presence of distinct structural features in the active site of the A-chain and in the 2gamma sugar-binding site of the B-chain. The conformation of the side chain of Tyr110, which is a conserved active-site residue in the A subunit, is strikingly different from those observed in other mistletoe RIPs, indicating its unique substrate-binding preference. The deletion of two important residues from the kink region after Ala231 in the 2gamma subdomain of the B-chain results in a significantly different conformation of the sugar-binding pocket. A ribosome-recognition site has also been identified in HmRip. The site is a shallow cavity, with the conserved residues Arg51, Asp70, Thr72 and Asn73 involved in the binding. The conformations of the antigenic epitopes of residues 1-20, 85-103 and 206-223 differ from those observed in other type II RIPs, resulting in the distinct antigenicity and pharmacological properties of HmRip.
About this Structure
1PC8 is a Protein complex structure of sequences from Viscum album. Full crystallographic information is available from OCA.
Reference
Structure of a novel ribosome-inactivating protein from a hemi-parasitic plant inhabiting the northwestern Himalayas., Mishra V, Ethayathulla AS, Sharma RS, Yadav S, Krauspenhaar R, Betzel C, Babu CR, Singh TP, Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 2):2295-304., Epub 2004 Nov 26. PMID:15583377 Page seeded by OCA on Sat May 3 04:55:46 2008
