5M99
Functional Characterization and Crystal Structure of Thermostable Amylase from Thermotoga petrophila, reveals High Thermostability and an Archaic form of Dimerization
Summary for 5M99
| Entry DOI | 10.2210/pdb5m99/pdb |
| Descriptor | Alpha-amylase, SODIUM ION, POTASSIUM ION, ... (8 entities in total) |
| Functional Keywords | hydrolase glycosyl hydrolase 13 family alpha amylase activity, hydrolase |
| Biological source | Thermotoga petrophila RKU-1 More |
| Total number of polymer chains | 2 |
| Total formula weight | 120597.68 |
| Authors | Hameed, U.,Price, I.,Mirza, O.A. (deposition date: 2016-11-01, release date: 2017-07-19, Last modification date: 2024-05-08) |
| Primary citation | Hameed, U.,Price, I.,Ke, A.,Wilson, D.B.,Mirza, O. Functional characterization and crystal structure of thermostable amylase from Thermotoga petrophila, reveals high thermostability and an unusual form of dimerization. Biochim. Biophys. Acta, 1865:1237-1245, 2017 Cited by PubMed Abstract: Thermostable α-amylases have many industrial applications and are therefore continuously explored from novel sources. We present the characterization of a novel putative α-amylase gene product (Tp-AmyS) cloned from Thermotoga petrophila. The purified recombinant enzyme is highly thermostable and able to hydrolyze starch into dextrin between 90 and 100°C, with optimum activity at 98°C and pH8.5. The activity increased in the presence of Rb, K and Ca ions, whereas other ions inhibited activity. The crystal structure of Tp-AmyS at 1.7Å resolution showed common features of the GH-13 family, however was apparently found to be a dimer. Several residues from one monomer interacted with a docked acarbose, an inhibitor of Tp-AmyS, in the other monomer, suggesting catalytic cooperativity within the dimer. The most striking feature of the dimer was that it resembled the dimerization of salivary amylase from a previous crystal structure, and thus could be a functional feature of some amylases. PubMed: 28648523DOI: 10.1016/j.bbapap.2017.06.015 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.96 Å) |
Structure validation
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