2gjr
From Proteopedia
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|PDB= 2gjr |SIZE=350|CAPTION= <scene name='initialview01'>2gjr</scene>, resolution 2.10Å | |PDB= 2gjr |SIZE=350|CAPTION= <scene name='initialview01'>2gjr</scene>, resolution 2.10Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1w9x|1W9X]], [[2gjp|2GJP]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gjr OCA], [http://www.ebi.ac.uk/pdbsum/2gjr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gjr RCSB]</span> | ||
}} | }} | ||
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[[Category: Kaasgaard, S G.]] | [[Category: Kaasgaard, S G.]] | ||
[[Category: Lyhne-Iversen, L.]] | [[Category: Lyhne-Iversen, L.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: NA]] | ||
[[Category: alpha-amylase]] | [[Category: alpha-amylase]] | ||
[[Category: bacillus halmapalus]] | [[Category: bacillus halmapalus]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:17:35 2008'' |
Revision as of 00:17, 31 March 2008
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| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | Alpha-amylase, with EC number 3.2.1.1 | ||||||
| Related: | 1W9X, 2GJP
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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