8JJM
X-ray crystal structure of a multifunctional enzyme (Amy63) from Vibrio alginolyticus 63
Summary for 8JJM
| Entry DOI | 10.2210/pdb8jjm/pdb |
| Descriptor | Amy63, CALCIUM ION, SODIUM ION, ... (5 entities in total) |
| Functional Keywords | amylase, hydrolase |
| Biological source | Vibrio alginolyticus |
| Total number of polymer chains | 2 |
| Total formula weight | 112542.28 |
| Authors | |
| Primary citation | Sun, Y.,Liu, G.,Liu, G.,Tang, H.,Sun, C.,Zhang, W.,Chen, L. The novel amylase function of the carboxyl terminal domain of Amy63. Biochem.Biophys.Res.Commun., 671:10-17, 2023 Cited by PubMed Abstract: α-amylase plays a crucial role in regulating metabolism and health by hydrolyzing of starch and glycogen. Despite comprehensive studies of this classic enzyme spanning over a century, the function of its carboxyl terminal domain (CTD) with a conserved eight β-strands is still not fully understood. Amy63, identified from a marine bacterium, was reported as a novel multifunctional enzyme with amylase, agarase and carrageenase activities. In this study, the crystal structure of Amy63 was determined at 1.8 Å resolution, revealing high conservation with some other amylases. Interestingly, the independent amylase activity of the carboxyl terminal domain of Amy63 (Amy63_CTD) was newly discovered by the plate-based assay and mass spectrometry. To date, the Amy63_CTD alone could be regarded as the smallest amylase subunit. Moreover, the significant amylase activity of Amy63_CTD was measured over a wide range of temperature and pH, with optimal activity at 60 °C and pH 7.5. The Small-angle X-ray scattering (SAXS) data showed that the high-order oligomeric assembly gradually formed with increasing concentration of Amy63_CTD, implying the novel catalytic mechanism as revealed by the assembly structure. Therefore, the discovery of the novel independent amylase activity of Amy63_CTD suggests a possible missing step or a new perspective in the complex catalytic process of Amy63 and other related α-amylases. This work may shed light on the design of nanozymes to process marine polysaccharides efficiently. PubMed: 37290279DOI: 10.1016/j.bbrc.2023.05.071 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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