Crystal structure of Anoxybacillus α-amylase provides insights into maltose binding of a new glycosyl hydrolase subclass
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 rep...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Publishing Group
2016
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| Online Access: | http://psasir.upm.edu.my/id/eprint/43395/1/43395.pdf |
| _version_ | 1796974334461345792 |
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| author | Chai, Kian Piaw Othman, Noor Farhan Teh, Aik Hong Ho, Kok Lian Chan, Kok Gan Shamsir, Mohd Shahir Goh, Kian Mau Ng, Chyan Leong |
| author_facet | Chai, Kian Piaw Othman, Noor Farhan Teh, Aik Hong Ho, Kok Lian Chan, Kok Gan Shamsir, Mohd Shahir Goh, Kian Mau Ng, Chyan Leong |
| author_sort | Chai, Kian Piaw |
| collection | UPM |
| description | 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 Ca2+ ion supplementation enhances the catalytic activities of ASKA and TASKA. The crystal structures reveal the presence of four Ca2+ 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. |
| first_indexed | 2024-03-06T08:55:32Z |
| format | Article |
| id | upm.eprints-43395 |
| institution | Universiti Putra Malaysia |
| language | English |
| last_indexed | 2024-03-06T08:55:32Z |
| publishDate | 2016 |
| publisher | Nature Publishing Group |
| record_format | dspace |
| spelling | upm.eprints-433952016-05-19T01:52:40Z http://psasir.upm.edu.my/id/eprint/43395/ Crystal structure of Anoxybacillus α-amylase provides insights into maltose binding of a new glycosyl hydrolase subclass Chai, Kian Piaw Othman, Noor Farhan Teh, Aik Hong Ho, Kok Lian Chan, Kok Gan Shamsir, Mohd Shahir Goh, Kian Mau Ng, Chyan Leong 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 Ca2+ ion supplementation enhances the catalytic activities of ASKA and TASKA. The crystal structures reveal the presence of four Ca2+ 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. Nature Publishing Group 2016 Article PeerReviewed application/pdf en http://psasir.upm.edu.my/id/eprint/43395/1/43395.pdf Chai, Kian Piaw and Othman, Noor Farhan and Teh, Aik Hong and Ho, Kok Lian and Chan, Kok Gan and Shamsir, Mohd Shahir and Goh, Kian Mau and Ng, Chyan Leong (2016) Crystal structure of Anoxybacillus α-amylase provides insights into maltose binding of a new glycosyl hydrolase subclass. Scientific Reports, 6. art. no. 23126. pp. 1-10. ISSN 2045-2322 10.1038/srep23126 |
| spellingShingle | Chai, Kian Piaw Othman, Noor Farhan Teh, Aik Hong Ho, Kok Lian Chan, Kok Gan Shamsir, Mohd Shahir Goh, Kian Mau Ng, Chyan Leong Crystal structure of Anoxybacillus α-amylase provides insights into maltose binding of a new glycosyl hydrolase subclass |
| title | Crystal structure of Anoxybacillus α-amylase provides insights into maltose binding of a new glycosyl hydrolase subclass |
| title_full | Crystal structure of Anoxybacillus α-amylase provides insights into maltose binding of a new glycosyl hydrolase subclass |
| title_fullStr | Crystal structure of Anoxybacillus α-amylase provides insights into maltose binding of a new glycosyl hydrolase subclass |
| title_full_unstemmed | Crystal structure of Anoxybacillus α-amylase provides insights into maltose binding of a new glycosyl hydrolase subclass |
| title_short | Crystal structure of Anoxybacillus α-amylase provides insights into maltose binding of a new glycosyl hydrolase subclass |
| title_sort | crystal structure of anoxybacillus α amylase provides insights into maltose binding of a new glycosyl hydrolase subclass |
| url | http://psasir.upm.edu.my/id/eprint/43395/1/43395.pdf |
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