2gjp: Difference between revisions

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[[Image:2gjp.gif|left|200px]]
{{Seed}}
[[Image:2gjp.png|left|200px]]


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{{STRUCTURE_2gjp|  PDB=2gjp  |  SCENE=  }}  
{{STRUCTURE_2gjp|  PDB=2gjp  |  SCENE=  }}  


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




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Bacillus halmapalus]]
[[Category: Bacillus halmapalus]]
[[Category: Maltose binding site]]
[[Category: Maltose binding site]]
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