4YP2

Cleavage of nicotinamide adenine dinucleotides by the ribosome inactivating protein from Momordica charantia

Summary for 4YP2

• Entry DOI: 10.2210/pdb4yp2/pdb
• Related: 1MOM
• Descriptor: Ribosome-inactivating protein momordin I, 2-acetamido-2-deoxy-beta-D-glucopyranose, NICOTINAMIDE, ... (4 entities in total)
• Functional Keywords: ribosome inactivating protein, n-glycosidase, nicotinamide, complex, hydrolase
• Biological source: Momordica charantia (Bitter gourd)
• Total number of polymer chains: 1
• Total formula weight: 27739.62

Authors

Vinkovic, M.,Hussain, J.,Wood, G.E.,Gill, R.,Wood, S.P. (deposition date: 2015-03-12, release date: 2015-05-20, Last modification date: 2024-11-13)

Primary citation

Vinkovic, M.,Dunn, G.,Wood, G.E.,Husain, J.,Wood, S.P.,Gill, R.
Cleavage of nicotinamide adenine dinucleotide by the ribosome-inactivating protein from Momordica charantia.
Acta Crystallogr.,Sect.F, 71:1152-1155, 2015

PubMed Abstract: The interaction of momordin, a type 1 ribosome-inactivating protein from Momordica charantia, with NADP(+) and NADPH has been investigated by X-ray diffraction analysis of complexes generated by co-crystallization and crystal soaking. It is known that the proteins of this family readily cleave the adenine-ribose bond of adenosine and related nucleotides in the crystal, leaving the product, adenine, bound to the enzyme active site. Surprisingly, the nicotinamide-ribose bond of oxidized NADP(+) is cleaved, leaving nicotinamide bound in the active site in the same position but in a slightly different orientation to that of the five-membered ring of adenine. No binding or cleavage of NADPH was observed at pH 7.4 in these experiments. These observations are in accord with current views of the enzyme mechanism and may contribute to ongoing searches for effective inhibitors.

PubMed: 26323301
DOI: 10.1107/S2053230X15013540

Experimental method

X-RAY DIFFRACTION (1.35 Å)