5cf9 | pdb_00005cf9

Cleavage of nicotinamide adenine dinucleotide by the ribosome inactivating protein of Momordica charantia - enzyme-NADP+ co-crystallisation.

spinqualitylabelsall models 5cf9, resolution 1.52Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5cf9 is a 1 chain structure with sequence from Momordica charantia. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.52Å Ligands: NAG, NCA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RIP1_MOMCH Publication Abstract from PubMed 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. Cleavage of nicotinamide adenine dinucleotide by the ribosome-inactivating protein from Momordica charantia.,Vinkovic M, Dunn G, Wood GE, Husain J, Wood SP, Gill R Acta Crystallogr F Struct Biol Commun. 2015 Sep 1;71(Pt 9):1152-5. doi:, 10.1107/S2053230X15013540. Epub 2015 Aug 25. PMID:26323301 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosome inactivating protein 3D structures

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