6LOZ
crystal structure of alpha-momorcharin in complex with adenine
Summary for 6LOZ
| Entry DOI | 10.2210/pdb6loz/pdb |
| Descriptor | Ribosome-inactivating protein momordin I, ADENINE, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | alpha-momorcharin, ribosome-inactivating protein, rrna n-glycosidase, adenine, plant protein |
| Biological source | Momordica charantia (Bitter gourd) |
| Total number of polymer chains | 1 |
| Total formula weight | 31919.30 |
| Authors | |
| Primary citation | Fan, X.,Wang, Y.,Guo, F.,Zhang, Y.,Jin, T. Atomic-resolution structures of type I ribosome inactivating protein alpha-momorcharin with different substrate analogs. Int.J.Biol.Macromol., 164:265-276, 2020 Cited by PubMed Abstract: Alpha-momorcharin (Alpha-MMC) from the seed of bitter melon is a type I ribosome inactivating protein (RIP) that removes a specific adenine from 28S rRNA and inhibits protein biosynthesis. Here, we report seven crystal complex structures of alpha-MMC with different substrate analogs (adenine, AMP, cAMP, dAMP, ADP, GMP, and xanthosine) at 1.08 Å to 1.52 Å resolution. These structures reveal that not only adenine, but also guanine and their analogs can effectively bind to alpha-MMC. The side chain of Tyr93 adopts two conformations, serving as a switch to open and close the substrate binding pocket of alpha-MMC. Although adenine, AMP, GMP, and guanine are located in a similar active site in different RIPs, residues involved in the interaction between RIPs and substrate analogs are slightly different. Complex structures of alpha-MMC with different substrate analogs solved in this study provide useful information on its enzymatic mechanisms and may enable the development of new inhibitors to treat the poisoning of alpha-MMC. PubMed: 32653369DOI: 10.1016/j.ijbiomac.2020.07.063 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.08 Å) |
Structure validation
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