1TCS

CRYSTAL STRUCTURE OF TRICHOSANTHIN-NADPH COMPLEX AT 1.7 ANGSTROMS RESOLUTION REVEALS ACTIVE-SITE ARCHITECTURE

Summary for 1TCS

• Entry DOI: 10.2210/pdb1tcs/pdb
• Descriptor: TRICHOSANTHIN, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• Functional Keywords: toxin, protein synthesis inhibitor
• Biological source: Trichosanthes kirilowii
• Total number of polymer chains: 1
• Total formula weight: 27912.19

Authors

Xiong, J.-P.,Xia, Z.-X.,Wang, Y. (deposition date: 1994-12-27, release date: 1995-07-10, Last modification date: 2024-02-14)

Primary citation

Xiong, J.P.,Xia, Z.X.,Wang, Y.
Crystal structure of trichosanthin-NADPH complex at 1.7 A resolution reveals active-site architecture.
Nat.Struct.Biol., 1:695-700, 1994

PubMed Abstract: We describe here the crystal structure of the trichosanthin-NADPH complex determined at a resolution of 1.7 A. The adenine base stacks between Tyr 70 and Tyr 111. Arg 163, Glu 160 and Tyr 70 form hydrogen bonds to N(3), O(3') and, through a water molecule, to N(9) of adenosine, respectively. This is the first high resolution structure of a complex between a ribosome-inactivating protein and a substrate analogue, in which the electron density of the N-glycosidic bond is well defined and the preassociated water, thought to be responsible for hydrolyzing the N-C bond, is also explicitly elucidated.

PubMed: 7634073
DOI: 10.1038/nsb1094-695

Experimental method

X-RAY DIFFRACTION (1.7 Å)