2gjr
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(New page: 200px<br /><applet load="2gjr" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gjr, resolution 2.10Å" /> '''Structure of bacillu...)
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Revision as of 09:07, 21 November 2007
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Structure of bacillus halmapalus alpha-amylase without any substrate analogues
Overview
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.
About this Structure
2GJR is a Single protein structure of sequence from Bacillus halmapalus with CA, NA and ACT as ligands. Active as Alpha-amylase, with EC number 3.2.1.1 Full crystallographic information is available from OCA.
Reference
Structure of Bacillus halmapalus alpha-amylase crystallized with and without the substrate analogue acarbose and maltose., Lyhne-Iversen L, Hobley TJ, Kaasgaard SG, Harris P, Acta Crystallograph Sect F Struct Biol Cryst Commun. 2006 Sep 1;62(Pt, 9):849-54. Epub 2006 Aug 26. PMID:16946462
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