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1PC8

Crystal Structure of a novel form of mistletoe lectin from Himalayan Viscum album L. at 3.8A resolution

Summary for 1PC8
Entry DOI10.2210/pdb1pc8/pdb
Related1MQC
DescriptorHimalayan mistletoe ribosome-inactivating protein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
Functional Keywordsnovel form, mistletoe lectin, hydrolase
Biological sourceViscum album (European mistletoe)
More
Total number of polymer chains2
Total formula weight55857.11
Authors
Mishra, V.,Ethayathulla, A.S.,Paramasivam, M.,Singh, G.,Yadav, S.,Kaur, P.,Sharma, R.S.,Babu, C.R.,Singh, T.P. (deposition date: 2003-05-16, release date: 2004-06-22, Last modification date: 2024-10-30)
Primary citationMishra, V.,Ethayathulla, A.S.,Sharma, R.S.,Yadav, S.,Krauspenhaar, R.,Betzel, C.,Babu, C.R.,Singh, T.P.
Structure of a novel ribosome-inactivating protein from a hemi-parasitic plant inhabiting the northwestern Himalayas.
Acta Crystallogr.,Sect.D, 60:2295-2304, 2004
Cited by
PubMed Abstract: 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.
PubMed: 15583377
DOI: 10.1107/S0907444904023534
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.8 Å)
Structure validation

226707

數據於2024-10-30公開中

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