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[[Image:2gjp.png|left|200px]]
==Structure of Bacillus halmapalus alpha-amylase, crystallized with the substrate analogue acarbose and maltose==
<StructureSection load='2gjp' size='340' side='right' caption='[[2gjp]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2gjp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_halmapalus Bacillus halmapalus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GJP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2GJP FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=DAF:4,6-DIDEOXY-4-{[(1S,5R,6S)-3-FORMYL-5,6-DIHYDROXY-4-OXOCYCLOHEX-2-EN-1-YL]AMINO}-ALPHA-D-XYLO-HEX-5-ENOPYRANOSE'>DAF</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w9x|1w9x]], [[2gjr|2gjr]]</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gjp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2gjp RCSB], [http://www.ebi.ac.uk/pdbsum/2gjp PDBsum]</span></td></tr>
<table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gj/2gjp_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


{{STRUCTURE_2gjp|  PDB=2gjp  |  SCENE=  }}
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<ref>PMID:16946462</ref>


===Structure of Bacillus halmapalus alpha-amylase, crystallized with the substrate analogue acarbose and maltose===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_16946462}}
 
==About this Structure==
[[2gjp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_halmapalus Bacillus halmapalus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GJP OCA].


==See Also==
==See Also==
*[[Alpha-Amylase|Alpha-Amylase]]
*[[Amylase|Amylase]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:016946462</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Alpha-amylase]]
[[Category: Alpha-amylase]]
[[Category: Bacillus halmapalus]]
[[Category: Bacillus halmapalus]]
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