1nli
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ADE:ADENINE'>ADE</scene> | |LIGAND= <scene name='pdbligand=ADE:ADENINE'>ADE</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= 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]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |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.]] | ||
- | [[Category: ADE]] | ||
[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
[[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 Sun Mar 30 22:31:59 2008'' |
Revision as of 19:32, 30 March 2008
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, resolution 1.93Å | |||||||
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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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