1pc8

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[[Image:1pc8.gif|left|200px]]<br /><applet load="1pc8" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1pc8.gif|left|200px]]
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caption="1pc8, resolution 3.80&Aring;" />
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'''Crystal Structure of a novel form of mistletoe lectin from Himalayan Viscum album L. at 3.8A resolution'''<br />
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{{Structure
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|PDB= 1pc8 |SIZE=350|CAPTION= <scene name='initialview01'>1pc8</scene>, resolution 3.80&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22]
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|GENE=
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}}
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'''Crystal Structure of a novel form of mistletoe lectin from Himalayan Viscum album L. at 3.8A resolution'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1PC8 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Viscum_album Viscum album] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/rRNA_N-glycosylase rRNA N-glycosylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.22 3.2.2.22] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PC8 OCA].
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1PC8 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Viscum_album Viscum album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PC8 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15583377 15583377]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15583377 15583377]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Viscum album]]
[[Category: Viscum album]]
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[[Category: novel form]]
[[Category: novel form]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:22:36 2008''

Revision as of 11:22, 20 March 2008


PDB ID 1pc8

Drag the structure with the mouse to rotate
, resolution 3.80Å
Ligands:
Activity: rRNA N-glycosylase, with EC number 3.2.2.22
Coordinates: save as pdb, mmCIF, xml



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

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