2q3n

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[[Image:2q3n.gif|left|200px]]<br /><applet load="2q3n" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2q3n.gif|left|200px]]
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caption="2q3n, resolution 3.50&Aring;" />
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'''Agglutinin from Abrus Precatorius (APA-I)'''<br />
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{{Structure
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|PDB= 2q3n |SIZE=350|CAPTION= <scene name='initialview01'>2q3n</scene>, resolution 3.50&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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'''Agglutinin from Abrus Precatorius (APA-I)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2Q3N is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Abrus_precatorius Abrus precatorius] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 2AMZ. 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=2Q3N OCA].
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2Q3N is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Abrus_precatorius Abrus precatorius]. This structure supersedes the now removed PDB entry 2AMZ. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q3N OCA].
==Reference==
==Reference==
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Structure-function analysis and insights into the reduced toxicity of Abrus precatorius agglutinin I in relation to abrin., Bagaria A, Surendranath K, Ramagopal UA, Ramakumar S, Karande AA, J Biol Chem. 2006 Nov 10;281(45):34465-74. Epub 2006 Jun 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16772301 16772301]
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Structure-function analysis and insights into the reduced toxicity of Abrus precatorius agglutinin I in relation to abrin., Bagaria A, Surendranath K, Ramagopal UA, Ramakumar S, Karande AA, J Biol Chem. 2006 Nov 10;281(45):34465-74. Epub 2006 Jun 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16772301 16772301]
[[Category: Abrus precatorius]]
[[Category: Abrus precatorius]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: ribosome-inactivating protein]]
[[Category: ribosome-inactivating protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:35:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:21:13 2008''

Revision as of 16:21, 20 March 2008


PDB ID 2q3n

Drag the structure with the mouse to rotate
, resolution 3.50Å
Ligands:
Activity: rRNA N-glycosylase, with EC number 3.2.2.22
Coordinates: save as pdb, mmCIF, xml



Agglutinin from Abrus Precatorius (APA-I)


Overview

Abrin and agglutinin-I from the seeds of Abrus precatorius are type II ribosome-inactivating proteins that inhibit protein synthesis in eukaryotic cells. The two toxins share a high degree of sequence similarity; however, agglutinin-I is weaker in its activity. We compared the kinetics of protein synthesis inhibition by abrin and agglutinin-I in two different cell lines and found that approximately 200-2000-fold higher concentration of agglutinin-I is needed for the same degree of inhibition. Like abrin, agglutinin-I also induced apoptosis in the cells by triggering the intrinsic mitochondrial pathway, although at higher concentrations as compared with abrin. The reason for the decreased toxicity of agglutinin-I became apparent on the analysis of the crystal structure of agglutinin-I obtained by us in comparison with that of the reported structure of abrin. The overall protein folding of agglutinin-I is similar to that of abrin-a with a single disulfide bond holding the toxic A subunit and the lectin-like B-subunit together, constituting a heterodimer. However, there are significant differences in the secondary structural elements, mostly in the A chain. The substitution of Asn-200 in abrin-a with Pro-199 in agglutinin-I seems to be a major cause for the decreased toxicity of agglutinin-I. This perhaps is not a consequence of any kink formation by a proline residue in the helical segment, as reported by others earlier, but due to fewer interactions that proline can possibly have with the bound substrate.

About this Structure

2Q3N is a Protein complex structure of sequences from Abrus precatorius. This structure supersedes the now removed PDB entry 2AMZ. Full crystallographic information is available from OCA.

Reference

Structure-function analysis and insights into the reduced toxicity of Abrus precatorius agglutinin I in relation to abrin., Bagaria A, Surendranath K, Ramagopal UA, Ramakumar S, Karande AA, J Biol Chem. 2006 Nov 10;281(45):34465-74. Epub 2006 Jun 13. PMID:16772301

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