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1NLI

Complex of [E160A-E189A] trichosanthin and adenine

Summary for 1NLI
Entry DOI10.2210/pdb1nli/pdb
DescriptorRibosome-inactivating protein alpha-trichosanthin, ADENINE (3 entities in total)
Functional Keywordsprotein-dna complex, ribosome-inactivating protein, hydrolase
Biological sourceTrichosanthes kirilowii
Total number of polymer chains1
Total formula weight27317.02
Authors
Shaw, P.C.,Wong, K.B.,Chan, D.S.B.,Williams, R.L. (deposition date: 2003-01-07, release date: 2003-01-21, Last modification date: 2023-08-16)
Primary citationShaw, P.C.,Wong, K.B.,Chan, D.S.,Williams, R.L.
Structural basis for the interaction of [E160A-E189A]-trichosanthin with adenine.
Toxicon, 41:575-581, 2003
Cited by
PubMed Abstract: 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.
PubMed: 12676436
DOI: 10.1016/S0041-0101(02)00387-2
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.93 Å)
Structure validation

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