1hvx

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{{STRUCTURE_1hvx| PDB=1hvx | SCENE= }}
{{STRUCTURE_1hvx| PDB=1hvx | SCENE= }}
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'''BACILLUS STEAROTHERMOPHILUS ALPHA-AMYLASE'''
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===BACILLUS STEAROTHERMOPHILUS ALPHA-AMYLASE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11226887 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11226887}}
==About this Structure==
==About this Structure==
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[[Category: Sodium]]
[[Category: Sodium]]
[[Category: Thermostability]]
[[Category: Thermostability]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:53:37 2008''

Revision as of 05:53, 1 July 2008

Image:1hvx.png

Template:STRUCTURE 1hvx

BACILLUS STEAROTHERMOPHILUS ALPHA-AMYLASE

Template:ABSTRACT PUBMED 11226887

About this Structure

1HVX is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

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:11226887

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