1nli

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|SITE=
|SITE=
|LIGAND= <scene name='pdbligand=ADE:ADENINE'>ADE</scene>
|LIGAND= <scene name='pdbligand=ADE:ADENINE'>ADE</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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|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= Trichosanthin ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3677 Trichosanthes kirilowii])
|GENE= Trichosanthin ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3677 Trichosanthes kirilowii])
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nli OCA], [http://www.ebi.ac.uk/pdbsum/1nli PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nli RCSB]</span>
}}
}}
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[[Category: Williams, R L.]]
[[Category: Williams, R L.]]
[[Category: Wong, K B.]]
[[Category: Wong, K B.]]
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[[Category: ADE]]
 
[[Category: protein-dna complex]]
[[Category: protein-dna complex]]
[[Category: ribosome-inactivating protein]]
[[Category: ribosome-inactivating protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:58:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:31:59 2008''

Revision as of 19:32, 30 March 2008


PDB ID 1nli

Drag the structure with the mouse to rotate
, resolution 1.93Å
Ligands:
Gene: Trichosanthin (Trichosanthes kirilowii)
Activity: rRNA N-glycosylase, with EC number 3.2.2.22
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Complex of [E160A-E189A] trichosanthin and adenine


Overview

Trichosanthin is a ribosome-inactivating protein that cleaves specifically the N-glycosidic bond of A-4324 of 28S rRNA. Trichosanthin and its variant [E160A-E189A]-trichosanthin were found to bind an adenine base with a K(d) value of approximately 0.2mM. To determine how this doubly mutated variant of trichosanthin interacts with adenine, the co-crystal structure of [E160A-E189A]-trichosanthin and adenine was resolved to 0.193nm which revealed that the active site conformation of the doubly mutated variant is isomorphous to wild-type trichosanthin. Water molecules were found at locations corresponding to the eliminated side chain of Glu-160 and Glu-189. On the other hand, the adenine base interacted with [E160A-E189A]-trichosanthin in a manner similar to that in wild-type trichosanthin. Our structural analysis illustrates that Glu-160 and Glu-189 in trichosanthin do not play an important role in maintaining the active site conformation and binding adenine, an essential step for substrate-enzyme interaction. On the other hand, removal of two glutamate residues changed a large patch of negatively charged surface to a positive charge, which may account for the destabilization of the oxocarbenium-like transition-state and the significant decrease in ribosome-inactivating activity in [E160A-E189A]-trichosanthin.

About this Structure

1NLI is a Single protein structure of sequence from Trichosanthes kirilowii. Full crystallographic information is available from OCA.

Reference

Structural basis for the interaction of [E160A-E189A]-trichosanthin with adenine., Shaw PC, Wong KB, Chan DS, Williams RL, Toxicon. 2003 Apr;41(5):575-81. PMID:12676436

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