1hvx: Difference between revisions
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[[Image:1hvx.gif|left|200px]] | [[Image:1hvx.gif|left|200px]] | ||
'''BACILLUS STEAROTHERMOPHILUS ALPHA-AMYLASE''' | {{Structure | ||
|PDB= 1hvx |SIZE=350|CAPTION= <scene name='initialview01'>1hvx</scene>, resolution 2.0Å | |||
|SITE= | |||
|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= AMYT631 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 Geobacillus stearothermophilus]) | |||
}} | |||
'''BACILLUS STEAROTHERMOPHILUS ALPHA-AMYLASE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1HVX is a [ | 1HVX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HVX OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of Bacillus stearothermophilus alpha-amylase: possible factors determining the thermostability., Suvd D, Fujimoto Z, Takase K, Matsumura M, Mizuno H, J Biochem. 2001 Mar;129(3):461-8. PMID:[http:// | Crystal structure of Bacillus stearothermophilus alpha-amylase: possible factors determining the thermostability., Suvd D, Fujimoto Z, Takase K, Matsumura M, Mizuno H, J Biochem. 2001 Mar;129(3):461-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11226887 11226887] | ||
[[Category: Alpha-amylase]] | [[Category: Alpha-amylase]] | ||
[[Category: Geobacillus stearothermophilus]] | [[Category: Geobacillus stearothermophilus]] | ||
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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 11:42:14 2008'' | ||
Revision as of 12:42, 20 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | AMYT631 (Geobacillus stearothermophilus) | ||||||
| Activity: | Alpha-amylase, with EC number 3.2.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BACILLUS STEAROTHERMOPHILUS ALPHA-AMYLASE
OverviewOverview
The crystal structure of a thermostable alpha-amylase from Bacillus stearothermophilus (BSTA) has been determined at 2.0 A resolution. The main-chain fold is almost identical to that of the known crystal structure of Bacillus licheniformis alpha-amylase (BLA). BLA is known to be more stable than BSTA. A structural comparison between the crystal structures of BSTA and BLA showed significant differences that may account for the difference in their thermostabilities, as follows. (i) The two-residue insertion in BSTA, Ile181-Gly182, pushes away the spatially contacting region including Asp207, which corresponds to Ca(2+)-coordinating Asp204 in BLA. As a result, Asp207 cannot coordinate the Ca(2+). (ii) BSTA contains nine fewer hydrogen bonds than BLA, which costs about 12 kcal/mol. This tendency is prominent in the (beta/alpha)(8)-barrel, where 10 fewer hydrogen bonds were observed in BSTA. BLA forms a denser hydrogen bond network in the inter-helical region, which may stabilize alpha-helices in the barrel. (iii) A few small voids observed in the alpha-helical region of the (beta/alpha)(8)-barrel in BSTA decrease inter-helical compactness and hydrophobic interactions. (iv) The solvent-accessible surface area of charged residues in BLA is about two times larger than that in BSTA.
About this StructureAbout this Structure
1HVX is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of Bacillus stearothermophilus alpha-amylase: possible factors determining the thermostability., Suvd D, Fujimoto Z, Takase K, Matsumura M, Mizuno H, J Biochem. 2001 Mar;129(3):461-8. PMID:11226887
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