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2gjp
From Proteopedia
(New page: 200px<br /><applet load="2gjp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gjp, resolution 1.90Å" /> '''Structure of Bacillu...) |
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| - | [[Image:2gjp.gif|left|200px]]<br /><applet load="2gjp" size=" | + | [[Image:2gjp.gif|left|200px]]<br /><applet load="2gjp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2gjp, resolution 1.90Å" /> | caption="2gjp, resolution 1.90Å" /> | ||
'''Structure of Bacillus halmapalus alpha-amylase, crystallized with the substrate analogue acarbose and maltose'''<br /> | '''Structure of Bacillus halmapalus alpha-amylase, crystallized with the substrate analogue acarbose and maltose'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Recombinant Bacillus halmapalus alpha-amylase (BHA) was studied in two | + | 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== | ==About this Structure== | ||
| - | 2GJP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_halmapalus Bacillus halmapalus] with MAL, GLC, CA and NA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] Full crystallographic information is available from [http:// | + | 2GJP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_halmapalus Bacillus halmapalus] with <scene name='pdbligand=MAL:'>MAL</scene>, <scene name='pdbligand=GLC:'>GLC</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GJP OCA]. |
==Reference== | ==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 | + | 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 Crystallogr Sect F Struct Biol Cryst Commun. 2006 Sep 1;62(Pt, 9):849-54. Epub 2006 Aug 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16946462 16946462] |
[[Category: Alpha-amylase]] | [[Category: Alpha-amylase]] | ||
[[Category: Bacillus halmapalus]] | [[Category: Bacillus halmapalus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Harris, P.]] | [[Category: Harris, P.]] | ||
| - | [[Category: Hobley, T | + | [[Category: Hobley, T J.]] |
| - | [[Category: Kaasgaard, S | + | [[Category: Kaasgaard, S G.]] |
[[Category: Lyhne-Iversen, L.]] | [[Category: Lyhne-Iversen, L.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
| Line 26: | Line 26: | ||
[[Category: maltose binding site]] | [[Category: maltose binding site]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:32:25 2008'' |
Revision as of 15:32, 21 February 2008
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Structure of Bacillus halmapalus alpha-amylase, crystallized with the substrate analogue acarbose and maltose
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
2GJP is a Single protein structure of sequence from Bacillus halmapalus with , , and 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 Crystallogr Sect F Struct Biol Cryst Commun. 2006 Sep 1;62(Pt, 9):849-54. Epub 2006 Aug 26. PMID:16946462
Page seeded by OCA on Thu Feb 21 17:32:25 2008
Categories: Alpha-amylase | Bacillus halmapalus | Single protein | Harris, P. | Hobley, T J. | Kaasgaard, S G. | Lyhne-Iversen, L. | CA | GLC | MAL | NA | Maltose binding site
