1bli
From Proteopedia
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| - | [[Image:1bli.gif|left|200px]] | + | [[Image:1bli.gif|left|200px]] |
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| - | '''BACILLUS LICHENIFORMIS ALPHA-AMYLASE''' | + | {{Structure |
| + | |PDB= 1bli |SIZE=350|CAPTION= <scene name='initialview01'>1bli</scene>, resolution 1.90Å | ||
| + | |SITE= <scene name='pdbsite=CA1:Ca+Binding+Site.+This+Ca+Binding+Site+Is+Conserved+In+Al+...'>CA1</scene>, <scene name='pdbsite=CA2:Ca+Binding+Site.+This+Ca+Binding+Site+Is+Not+Conserved+I+...'>CA2</scene>, <scene name='pdbsite=CA3:Ca+Binding+Site.+This+Ca+Binding+Site+Located+In+The+Int+...'>CA3</scene>, <scene name='pdbsite=CS:Catalytic+Site'>CS</scene> and <scene name='pdbsite=NA1:Na+Binding+Site.+This+Is+The+First+Na+Binding+Site+Obser+...'>NA1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <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] | ||
| + | |GENE= AMYL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1402 Bacillus licheniformis]) | ||
| + | }} | ||
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| + | '''BACILLUS LICHENIFORMIS ALPHA-AMYLASE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BLI is a [ | + | 1BLI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BLI OCA]. |
==Reference== | ==Reference== | ||
| - | Activation of Bacillus licheniformis alpha-amylase through a disorder-->order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad., Machius M, Declerck N, Huber R, Wiegand G, Structure. 1998 Mar 15;6(3):281-92. PMID:[http:// | + | Activation of Bacillus licheniformis alpha-amylase through a disorder-->order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad., Machius M, Declerck N, Huber R, Wiegand G, Structure. 1998 Mar 15;6(3):281-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9551551 9551551] |
[[Category: Alpha-amylase]] | [[Category: Alpha-amylase]] | ||
[[Category: Bacillus licheniformis]] | [[Category: Bacillus licheniformis]] | ||
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[[Category: thermostability]] | [[Category: thermostability]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:12:37 2008'' |
Revision as of 08:12, 20 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , and | ||||||
| Ligands: | and | ||||||
| Gene: | AMYL (Bacillus licheniformis) | ||||||
| Activity: | Alpha-amylase, with EC number 3.2.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BACILLUS LICHENIFORMIS ALPHA-AMYLASE
Overview
BACKGROUND: The structural basis as to how metals regulate the functional state of a protein by altering or stabilizing its conformation has been characterized in relatively few cases because the metal-free form of the protein is often partially disordered and unsuitable for crystallographic analysis. This is not the case, however, for Bacillus licheniformis alpha-amylase (BLA) for which the structure of the metal-free form is available. BLA is a hyperthermostable enzyme which is widely used in biotechnology, for example in the breakdown of starch or as a component of detergents. The determination of the structure of BLA in the metal-containing form, together with comparisons to the apo enzyme, will help us to understand the way in which metal ions can regulate enzyme activity. RESULTS: We report here the crystal structure of native, metal-containing BLA. The structure shows that the calcium-binding site which is conserved in all alpha-amylases forms part of an unprecedented linear triadic metal array, with two calcium ions flanking a central sodium ion. A region around the metal triad comprising 21 residues exhibits a conformational change involving a helix unwinding and a disorder-->order transition compared to the structure of metal-free BLA. Another calcium ion, not previously observed in alpha-amylases, is located at the interface between domains A and C. CONCLUSIONS: We present a structural description of a major conformational rearrangement mediated by metal ions. The metal induced disorder-->order transition observed in BLA leads to the formation of the extended substrate-binding site and explains on a structural level the calcium dependency of alpha-amylases. Sequence comparisons indicate that the unique Ca-Na-Ca metal triad and the additional calcium ion located between domains A and C might be found exclusively in bacterial alpha-amylases which show increased thermostability. The information presented here may help in the rational design of mutants with enhanced performance in biotechnological applications.
About this Structure
1BLI is a Single protein structure of sequence from Bacillus licheniformis. Full crystallographic information is available from OCA.
Reference
Activation of Bacillus licheniformis alpha-amylase through a disorder-->order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad., Machius M, Declerck N, Huber R, Wiegand G, Structure. 1998 Mar 15;6(3):281-92. PMID:9551551
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