5A2B
Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass
Summary for 5A2B
| Entry DOI | 10.2210/pdb5a2b/pdb |
| Related | 5A2A 5A2C |
| Related PRD ID | PRD_900001 |
| Descriptor | ANOXYBACILLUS ALPHA-AMYLASE, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | hydrolase, calcium-binding site, geobacillus, glycosyl hydrolase |
| Biological source | ANOXYBACILLUS SP. |
| Total number of polymer chains | 1 |
| Total formula weight | 58667.01 |
| Authors | Ng, C.L.,Chai, K.P.,Othman, N.F.,Teh, A.H.,Ho, K.L.,Chan, K.G.,Goh, K.M. (deposition date: 2015-05-17, release date: 2016-03-30, Last modification date: 2024-01-10) |
| Primary citation | Chai, K.P.,Othman, N.F.B.,Teh, A.,Ho, K.L.,Chan, K.,Shamsir, M.S.,Goh, K.M.,Ng, C.L. Crystal Structure of Anoxybacillus Alpha-Amylase Provides Insights Into Maltose Binding of a New Glycosyl Hydrolase Subclass. Sci.Rep., 6:23126-, 2016 Cited by PubMed Abstract: A new subfamily of glycosyl hydrolase family GH13 was recently proposed for α-amylases from Anoxybacillus species (ASKA and ADTA), Geobacillus thermoleovorans (GTA, Pizzo, and GtamyII), Bacillus aquimaris (BaqA), and 95 other putative protein homologues. To understand this new GH13 subfamily, we report crystal structures of truncated ASKA (TASKA). ASKA is a thermostable enzyme capable of producing high levels of maltose. Unlike GTA, biochemical analysis showed that Ca(2+) ion supplementation enhances the catalytic activities of ASKA and TASKA. The crystal structures reveal the presence of four Ca(2+) ion binding sites, with three of these binding sites are highly conserved among Anoxybacillus α-amylases. This work provides structural insights into this new GH13 subfamily both in the apo form and in complex with maltose. Furthermore, structural comparison of TASKA and GTA provides an overview of the conformational changes accompanying maltose binding at each subsite. PubMed: 26975884DOI: 10.1038/SREP23126 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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