Structure of Bacillus Halmapalus Alpha-amylase Crystallized with and Without the Substrate Analogue Acarbose and Maltose.
From: Department of Chemistry, Technical University of Denmark, Building 207, DK-2800 Kgs. Lyngby, Denmark.
Acta crystallographica. Section F, Structural biology and crystallization communications
- Publish Date: Sep 2006
- ISSN: 1744-3091
- Volume: 62
- Issue: Pt 9
- Pages: 849-54
- Medium: Internet
- Language: English
- Citation (JAMA): Lyhne-Iversen Louise, Hobley Timothy J, Kaasgaard Svend G, et al. Structure of Bacillus Halmapalus Alpha-amylase Crystallized with and Without the Substrate Analogue Acarbose and Maltose.. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. Sep 2006;62:849-54
Abstract
Recombinant Bacillus halmapalus alpha-amylase (BHA) was studied in two different crystal forms. The first crystal form was obtained by crystallization of BHA at room temperature in the presence of acarbose and maltose; data were collected at cryogenic temperature to a resolution of 1.9 A. It was found that the crystal belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 47.0, b = 73.5, c = 151.1 A. A maltose molecule was observed and found to bind to BHA and previous reports of the binding of a nonasaccharide were confirmed. The second crystal form was obtained by pH-induced crystallization of BHA in a MES-HEPES-boric acid buffer (MHB buffer) at 303 K; the solubility of BHA in MHB has a retrograde temperature dependency and crystallization of BHA was only possible by raising the temperature to at least 298 K. Data were collected at cryogenic temperature to a resolution of 2.0 A. The crystal belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 38.6, b = 59.0, c = 209.8 A. The structure was solved using molecular replacement. The maltose-binding site is described and the two structures are compared. No significant changes were seen in the structure upon binding of the substrates.
Mesh Headings (Keywords): Acarbose, Bacillus, Bacterial Proteins, Binding Sites, Carrier Proteins, Crystallization, Crystallography, X-Ray, Maltose, Substrate Specificity, alpha-Amylase
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