1hvx

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[[Image:1hvx.gif|left|200px]]
 
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{{Structure
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==BACILLUS STEAROTHERMOPHILUS ALPHA-AMYLASE==
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|PDB= 1hvx |SIZE=350|CAPTION= <scene name='initialview01'>1hvx</scene>, resolution 2.0&Aring;
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<StructureSection load='1hvx' size='340' side='right'caption='[[1hvx]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
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<table><tr><td colspan='2'>[[1hvx]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HVX FirstGlance]. <br>
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|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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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|GENE= AMYT631 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 Geobacillus stearothermophilus])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hvx OCA], [https://pdbe.org/1hvx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hvx RCSB], [https://www.ebi.ac.uk/pdbsum/1hvx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hvx ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hvx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hvx OCA], [http://www.ebi.ac.uk/pdbsum/1hvx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hvx RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/AMY_GEOSE AMY_GEOSE]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hv/1hvx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hvx ConSurf].
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<div style="clear:both"></div>
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'''BACILLUS STEAROTHERMOPHILUS ALPHA-AMYLASE'''
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==See Also==
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*[[Amylase|Amylase]]
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*[[Amylase 3D structures|Amylase 3D structures]]
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==Overview==
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__TOC__
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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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</StructureSection>
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==About this Structure==
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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].
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==Reference==
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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]
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[[Category: Alpha-amylase]]
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[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Fujimoto, Z.]]
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[[Category: Fujimoto Z]]
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[[Category: Matsumura, M.]]
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[[Category: Matsumura M]]
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[[Category: Mizuno, H.]]
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[[Category: Mizuno H]]
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[[Category: Suvd, D.]]
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[[Category: Suvd D]]
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[[Category: Takase, K.]]
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[[Category: Takase K]]
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[[Category: alpha-1,4-glucan-4-glucanohydrolase]]
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[[Category: alpha-amylase,starch degradation]]
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[[Category: calcium]]
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[[Category: glycosyltransferase]]
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[[Category: hydrolase]]
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[[Category: sodium]]
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[[Category: thermostability]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:11:09 2008''
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Current revision

BACILLUS STEAROTHERMOPHILUS ALPHA-AMYLASE

PDB ID 1hvx

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