2gjp: Difference between revisions

<StructureSection load='2gjp' size='340' side='right'caption='[[2gjp]], [[Resolution|resolution]] 1.90&Aring;' scene=''>

<table><tr><td colspan='2'>[[2gjp]] 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=2GJP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GJP FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gjp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gjp OCA], [https://pdbe.org/2gjp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gjp RCSB], [https://www.ebi.ac.uk/pdbsum/2gjp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gjp ProSAT]</span></td></tr>

    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gj/2gjp_consurf.spt"</scriptWhenChecked>

    <text>to colour the structure by Evolutionary Conservation</text>

</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=2gjp ConSurf].

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 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>

==See Also==

*[[Amylase 3D structures|Amylase 3D structures]]

== References ==

<references/>

</StructureSection>

[[Category: Large Structures]]

[[Category: Sutcliffiella halmapala]]

[[Category: Harris P]]

[[Category: Hobley TJ]]

[[Category: Kaasgaard SG]]

[[Category: Lyhne-Iversen L]]