3VM7
Structure of an Alpha-Amylase from Malbranchea cinnamomea
Summary for 3VM7
| Entry DOI | 10.2210/pdb3vm7/pdb |
| Descriptor | Alpha-amylase, CALCIUM ION, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | malbranchea cinnamomea c -amylase cmodels, protein conformation, hydrolase |
| Biological source | Malbranchea cinnamomea |
| Total number of polymer chains | 1 |
| Total formula weight | 54595.87 |
| Authors | Zhou, P.,Hu, S.Q.,Zhou, Y.,Han, P.,Yang, S.Q.,Jiang, Z.Q. (deposition date: 2011-12-09, release date: 2013-05-29, Last modification date: 2024-11-20) |
| Primary citation | Han, P.,Zhou, P.,Hu, S.,Yang, S.,Yan, Q.,Jiang, Z.Q. A Novel Multifunctional alpha-Amylase from the Thermophilic Fungus Malbranchea cinnamomea: Biochemical Characterization and Three-Dimensional Structure. Appl Biochem Biotechnol., 170:420-435, 2013 Cited by PubMed Abstract: A novel α-amylase (McAmyA) from the thermophilic fungus, Malbranchea cinnamomea was purified, characterized and crystallized in the present study. McAmyA was purified to apparent homogeneity with a molecular mass of 60.3 kDa on SDS-PAGE. The enzyme exhibited maximal activity at pH 6.5 and was stable within pH 5.0-10.0. It was most active at 65 °C and was stable up to 50 °C. McAmyA was capable of hydrolyzing amylose, starch, amylopectin, pullulan, cyclodextrins and maltooligosaccharides. The full-length cDNA of an α-amylase gene (McAmyA) from the strain was cloned. McAmyA consisted of a 1,476-bp open reading frame encoding 492 amino acids. It displayed the highest amino acid sequence homology (less than 60 %) with the reported α-amylases. The crystal structure of McAmyA was solved at a resolution of 2.25 Å (PDB code 3VM7). The overall structure of McAmyA reveals three domains with ten α helices and 14 β strands, and the putative catalytic residues are positioned at domain A with somewhat different secondary structural circumstances compared with typical α-amylases. PubMed: 23536251DOI: 10.1007/s12010-013-0198-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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