1Z5P
Crystal structure of MTA/AdoHcy nucleosidase with a ligand-free purine binding site
Summary for 1Z5P
| Entry DOI | 10.2210/pdb1z5p/pdb |
| Related | 1Z5N 1Z5O |
| Descriptor | MTA/SAH nucleosidase, 3,6,9,12,15,18,21,24-OCTAOXAHEXACOSAN-1-OL, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | mixed alpha/beta, hydrolase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 26437.29 |
| Authors | Lee, J.E.,Smith, G.D.,Horvatin, C.,Huang, D.J.T.,Cornell, K.A.,Riscoe, M.K.,Howell, P.L. (deposition date: 2005-03-18, release date: 2005-10-04, Last modification date: 2023-08-23) |
| Primary citation | Lee, J.E.,Smith, G.D.,Horvatin, C.,Huang, D.J.T.,Cornell, K.A.,Riscoe, M.K.,Howell, P.L. Structural snapshots of MTA/AdoHcy nucleosidase along the reaction coordinate provide insights into enzyme and nucleoside flexibility during catalysis J.Mol.Biol., 352:559-574, 2005 Cited by PubMed Abstract: MTA/AdoHcy nucleosidase (MTAN) irreversibly hydrolyzes the N9-C1' bond in the nucleosides, 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (AdoHcy) to form adenine and the corresponding thioribose. MTAN plays a vital role in metabolic pathways involving methionine recycling, biological methylation, polyamine biosynthesis, and quorum sensing. Crystal structures of a wild-type (WT) MTAN complexed with glycerol, and mutant-enzyme and mutant-product complexes have been determined at 2.0A, 2.0A, and 2.1A resolution, respectively. The WT MTAN-glycerol structure provides a purine-free model and in combination with the previously solved thioribose-free MTAN-ADE structure, we now have separate apo structures for both MTAN binding subsites. The purine and thioribose-free states reveal an extensive enzyme-immobilized water network in their respective binding subsites. The Asp197Asn MTAN-MTA and Glu12Gln MTAN-MTR.ADE structures are the first enzyme-substrate and enzyme-product complexes reported for MTAN, respectively. These structures provide representative snapshots along the reaction coordinate and allow insight into the conformational changes of the enzyme and the nucleoside substrate. A "catalytic movie" detailing substrate binding, catalysis, and product release is presented. PubMed: 16109423DOI: 10.1016/j.jmb.2005.07.027 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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