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1nli
From Proteopedia
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[[Image:1nli.jpg|left|200px]] | [[Image:1nli.jpg|left|200px]] | ||
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'''Complex of [E160A-E189A] trichosanthin and adenine''' | '''Complex of [E160A-E189A] trichosanthin and adenine''' | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Trichosanthes kirilowii]] | [[Category: Trichosanthes kirilowii]] | ||
| - | [[Category: | + | [[Category: RRNA N-glycosylase]] |
[[Category: Chan, D S.B.]] | [[Category: Chan, D S.B.]] | ||
[[Category: Shaw, P C.]] | [[Category: Shaw, P C.]] | ||
[[Category: Williams, R L.]] | [[Category: Williams, R L.]] | ||
[[Category: Wong, K B.]] | [[Category: Wong, K B.]] | ||
| - | [[Category: | + | [[Category: Protein-dna complex]] |
| - | [[Category: | + | [[Category: Ribosome-inactivating protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:40:26 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 23:40, 2 May 2008
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 Page seeded by OCA on Sat May 3 02:40:26 2008
