8xx9 | pdb_00008xx9

Rhodothermus marinus alpha-amylase RmGH13_47A CBM48-A-B-C domains

spinqualitylabelsall models 8xx9, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8xx9 is a 1 chain structure with sequence from Rhodothermus marinus JCM 9785. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.55Å Ligands: CA, MES, MN, MPD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D0MDJ8_RHOM4 Publication Abstract from PubMed Glycoside hydrolase (GH) family 13 is among the main families of enzymes acting on starch; recently, subfamily 47 of GH13 (GH13_47) has been established. The crystal structure and function of a GH13_47 enzyme from Bacteroides ovatus has only been reported to date. This enzyme has alpha-amylase activity, while the GH13_47 enzymes comprise approximately 800-900 amino acid residues which are almost double those of typical alpha-amylases. It is important to know how different the GH13_47 enzymes are from other alpha-amylases. Rhodothermus marinus JCM9785, a thermophilic bacterium, possesses a gene for the GH13_47 enzyme, which is designated here as RmGH13_47A. Its structure has been predicted to be composed of seven domains: N1, N2, N3, A, B, C, and D. We constructed a plasmid encoding Gly266-Glu886, which contains the N3, A, B, and C domains and expressed the protein in Escherichia coli. The enzyme hydrolyzed starch and pullulan by a neopullulanase-type action. Additionally, the enzyme acted on maltotetraose, and saccharides with alpha-1,6-glucosidic linkages were observed in the products. Following the replacement of the catalytic residue Asp563 with Ala, the crystal structure of the variant D563A in complex with the enzymatic products from maltotetraose was determined; as a result, electron density for an alpha-1,6-branched pentasaccharide was observed in the catalytic pocket, and Ile762 and Asp763 interacted with the branched chain of the pentasaccharide. These findings suggest that RmGH13_47A is an alpha-amylase that prefers alpha-1,6-branched parts of starch to produce oligosaccharides. Structural basis for the recognition of alpha-1,6-branched alpha-glucan by GH13_47 alpha-amylase from Rhodothermus marinus.,Miyasaka Y, Yokoyama K, Kozono T, Kitano Y, Miyazaki T, Sakaguchi M, Nishikawa A, Tonozuka T Proteins. 2024 Aug;92(8):984-997. doi: 10.1002/prot.26695. Epub 2024 Apr 20. PMID:38641972 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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