Structure of the Novel Alpha-amylase Amyc from Thermotoga Maritima.
From: Abteilung Molekulare Strukturbiologie, Institut für Mikrobiologie und Genetik, Georg-August-Universität, Göttingen, Germany.
Acta crystallographica. Section D, Biological crystallography
- Publish Date: Mar 2006
- ISSN: 0907-4449
- Volume: 62
- Issue: Pt 3
- Pages: 262-70
- Medium: Print
- Language: English
- Citation (JAMA): Dickmanns Achim, Ballschmiter Meike, Liebl Wolfgang, et al. Structure of the Novel Alpha-amylase Amyc from Thermotoga Maritima.. Acta Crystallogr. D Biol. Crystallogr. Mar 2006;62:262-70
Abstract
alpha-Amylases are essential enzymes in alpha-glucan metabolism and catalyse the hydrolysis of long sugar polymers such as amylose and starch. The crystal structure of a previously unidentified amylase (AmyC) from the hyperthermophilic organism Thermotoga maritima was determined at 2.2 Angstroms resolution by means of MAD. AmyC lacks sequence similarity to canonical alpha-amylases, which belong to glycosyl hydrolase families 13, 70 and 77, but exhibits significant similarity to a group of as yet uncharacterized proteins in COG1543 and is related to glycerol hydrolase family 57 (GH-57). AmyC reveals features that are characteristic of alpha-amylases, such as a distorted TIM-barrel structure formed by seven beta-strands and alpha-helices (domain A), and two additional but less well conserved domains. The latter are domain B, which contains three helices inserted in the TIM-barrel after beta-sheet 2, and domain C, a five-helix region at the C-terminus. Interestingly, despite moderate sequence homology, structure comparison revealed significant similarities to a member of GH-57 with known three-dimensional structure, Thermococcus litoralis 4-glucanotransferase, and an even higher similarity to a structure of an enzyme of unknown function from Thermus thermophilus.
Mesh Headings (Keywords): Bacteria, Binding Sites, Cloning, Molecular, Crystallization, Genomics, Kinetics, Models, Molecular, Protein Conformation, Protein Structure, Quaternary, Selenomethionine, alpha-Amylase
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