2JMU
NMR structure of the mouse thiamine triphosphatase
Summary for 2JMU
| Entry DOI | 10.2210/pdb2jmu/pdb |
| NMR Information | BMRB: 15063 |
| Descriptor | Thiamine-triphosphatase (1 entity in total) |
| Functional Keywords | thiamine triphosphatase, structural genomics, protein structure initiative, psi, center for eukaryotic structural genomics, cesg, hydrolase |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 24243.12 |
| Authors | Song, J.,Markley, J.L.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2006-12-05, release date: 2006-12-19, Last modification date: 2024-05-08) |
| Primary citation | Song, J.,Bettendorff, L.,Tonelli, M.,Markley, J.L. Structural basis for the catalytic mechanism of mammalian 25-kDa thiamine triphosphatase. J.Biol.Chem., 283:10939-10948, 2008 Cited by PubMed Abstract: Mammalian soluble thiamine triphosphatase (ThTPase) is a 25-kDa cytosolic enzyme that specifically catalyzes the conversion of thiamine triphosphate (ThTP) to thiamine diphosphate and has an absolute requirement for divalent cations. We have investigated the kinetic properties of recombinant mouse thiamine triphosphatase (mThTPase) and determined its solution structure by NMR spectroscopy. Residues responsible for binding Mg(2+) and ThTP were determined from NMR titration experiments. The binding of Mg(2+) induced only a minor local conformational change, whereas ThTP binding was found to cause a more global conformational change. We derived a structural model for the mThTPase.ThTP.Mg(2+) ternary complex and concluded from this that whereas free mThTPase has an open cleft fold, the enzyme in the ternary complex adopts a tunnel fold. Our results provide a functional rationale for a number of conserved residues and suggest an essential role for Mg(2+) in catalysis. We propose a mechanism underlying the high substrate specificity of mThTPase and discuss the possible role of water molecules in enzymatic catalysis. PubMed: 18276586DOI: 10.1074/jbc.M709675200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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