2GJP

Structure of Bacillus halmapalus alpha-amylase, crystallized with the substrate analogue acarbose and maltose

Summary for 2GJP

• Entry DOI: 10.2210/pdb2gjp/pdb
• Related: 1W9X 2GJR
• Related PRD ID: PRD_900001
• Descriptor: alpha-amylase, 4,6-dideoxy-4-{[(1S,5R,6S)-3-formyl-5,6-dihydroxy-4-oxocyclohex-2-en-1-yl]amino}-alpha-D-xylo-hex-5-enopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose, 4,6-dideoxy-4-{[(1S,5R,6S)-3-formyl-5,6-dihydroxy-4-oxocyclohex-2-en-1-yl]amino}-alpha-D-xylo-hex-5-enopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (8 entities in total)
• Functional Keywords: alpha-amylase, maltose binding site, bacillus halmapalus, hydrolase
• Biological source: Bacillus halmapalus
• Total number of polymer chains: 1
• Total formula weight: 58028.28

Authors

Lyhne-Iversen, L.,Hobley, T.J.,Kaasgaard, S.G.,Harris, P. (deposition date: 2006-03-31, release date: 2006-09-05, Last modification date: 2023-08-30)

Primary citation

Lyhne-Iversen, L.,Hobley, T.J.,Kaasgaard, S.G.,Harris, P.
Structure of Bacillus halmapalus alpha-amylase crystallized with and without the substrate analogue acarbose and maltose.
Acta Crystallogr.,Sect.F, 62:849-854, 2006

PubMed 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.

PubMed: 16946462
DOI: 10.1107/S174430910603096X

Experimental method

X-RAY DIFFRACTION (1.9 Å)