2q3n
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | ||
| - | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2q3n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q3n OCA], [http://www.ebi.ac.uk/pdbsum/2q3n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2q3n RCSB]</span> | ||
}} | }} | ||
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[[Category: Ramakumar, S.]] | [[Category: Ramakumar, S.]] | ||
[[Category: Surendranath, K.]] | [[Category: Surendranath, K.]] | ||
| - | [[Category: NAG]] | ||
[[Category: agglutinin abrin]] | [[Category: agglutinin abrin]] | ||
[[Category: immunotoxin]] | [[Category: immunotoxin]] | ||
[[Category: ribosome-inactivating protein]] | [[Category: ribosome-inactivating protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:44:09 2008'' |
Revision as of 01:44, 31 March 2008
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| , resolution 3.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | rRNA N-glycosylase, with EC number 3.2.2.22 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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