5m99 | pdb_00005m99

Functional Characterization and Crystal Structure of Thermostable Amylase from Thermotoga petrophila, reveals High Thermostability and an Archaic form of Dimerization

spinqualitylabelsall models 5m99, resolution 1.96Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5m99 is a 2 chain structure with sequence from Thermotoga petrophila RKU-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.96Å Ligands: CA, EDO, K, NA, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A059TXD8_THEP1 Publication Abstract from PubMed Thermostable alpha-amylases have many industrial applications and are therefore continuously explored from novel sources. We present the characterization of a novel putative alpha-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 degrees C, with optimum activity at 98 degrees C and pH8.5. The activity increased in the presence of Rb1+, K1+ and Ca2+ ions, whereas other ions inhibited activity. The crystal structure of Tp-AmyS at 1.7A 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. Functional characterization and crystal structure of thermostable amylase from Thermotoga petrophila, reveals high thermostability and an unusual form of dimerization.,Hameed U, Price I, Ikram-Ul-Haq, Ke A, Wilson DB, Mirza O Biochim Biophys Acta. 2017 Jun 22;1865(10):1237-1245. doi:, 10.1016/j.bbapap.2017.06.015. PMID:28648523 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Amylase 3D structures

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