2gjr

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(New page: 200px<br /><applet load="2gjr" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gjr, resolution 2.10&Aring;" /> '''Structure of bacillu...)
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[[Image:2gjr.jpg|left|200px]]<br /><applet load="2gjr" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2gjr, resolution 2.10&Aring;" />
 
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'''Structure of bacillus halmapalus alpha-amylase without any substrate analogues'''<br />
 
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==Overview==
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==Structure of bacillus halmapalus alpha-amylase without any substrate analogues==
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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.
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<StructureSection load='2gjr' size='340' side='right'caption='[[2gjr]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2gjr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sutcliffiella_halmapala Sutcliffiella halmapala]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GJR FirstGlance]. <br>
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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]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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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=2gjr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gjr OCA], [https://pdbe.org/2gjr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gjr RCSB], [https://www.ebi.ac.uk/pdbsum/2gjr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gjr ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMT6_BACS7 AMT6_BACS7]
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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/gj/2gjr_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=2gjr ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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2GJR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_halmapalus Bacillus halmapalus] with CA, NA and ACT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GJR OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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 Crystallograph Sect F Struct Biol Cryst Commun. 2006 Sep 1;62(Pt, 9):849-54. Epub 2006 Aug 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16946462 16946462]
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</div>
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[[Category: Alpha-amylase]]
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<div class="pdbe-citations 2gjr" style="background-color:#fffaf0;"></div>
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[[Category: Bacillus halmapalus]]
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[[Category: Single protein]]
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[[Category: Harris, P.]]
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[[Category: Hobley, T.J.]]
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[[Category: Kaasgaard, S.G.]]
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[[Category: Lyhne-Iversen, L.]]
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[[Category: ACT]]
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[[Category: CA]]
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[[Category: NA]]
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[[Category: alpha-amylase]]
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[[Category: bacillus halmapalus]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:14:42 2007''
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==See Also==
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*[[Amylase 3D structures|Amylase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Sutcliffiella halmapala]]
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[[Category: Harris P]]
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[[Category: Hobley TJ]]
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[[Category: Kaasgaard SG]]
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[[Category: Lyhne-Iversen L]]

Current revision

Structure of bacillus halmapalus alpha-amylase without any substrate analogues

PDB ID 2gjr

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