5a2a | pdb_00005a2a

Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass

spinqualitylabelsall models 5a2a, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5a2a is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, CA Related: 5a2b, 5a2c Activity: Alpha-amylase, with EC number 3.2.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Publication Abstract from PubMed A new subfamily of glycosyl hydrolase family GH13 was recently proposed for alpha-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 alpha-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. Crystal structure of Anoxybacillus alpha-amylase provides insights into maltose binding of a new glycosyl hydrolase subclass.,Chai KP, Othman NF, Teh AH, Ho KL, Chan KG, Shamsir MS, Goh KM, Ng CL Sci Rep. 2016 Mar 15;6:23126. doi: 10.1038/srep23126. PMID:26975884 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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