2e9b

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[[Image:2e9b.jpg|left|200px]]
 
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==Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with maltose==
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The line below this paragraph, containing "STRUCTURE_2e9b", creates the "Structure Box" on the page.
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<StructureSection load='2e9b' size='340' side='right'caption='[[2e9b]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E9B FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 2.3&#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=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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=PRD_900009:alpha-maltotriose'>PRD_900009</scene></td></tr>
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{{STRUCTURE_2e9b| PDB=2e9b | SCENE= }}
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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=2e9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e9b OCA], [https://pdbe.org/2e9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e9b RCSB], [https://www.ebi.ac.uk/pdbsum/2e9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e9b ProSAT]</span></td></tr>
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</table>
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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/e9/2e9b_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2e9b 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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The AmyX gene encoding pullulanase from the common spore-forming bacterium Bacillus subtilis strain 168 was cloned, overexpressed in Escherichia coli, purified and crystallized. The recombinant pullulanase was purified to homogeneity using ammonium sulfate precipitation, hydrophobic chromatography and anion-exchange chromatography, resulting in a specific activity of 24.10 U per milligram of protein. SDS-PAGE analysis showed that the molecular weight of the protein is approximately 81.0 kDa, which is similar to the calculated molecular weight, 81.1 kDa, from its translated cDNA sequence. The k(cat) and K(m) of the purified enzyme with pullulan as substrate were approximately 79 s(-1) and 1.284 mg ml(-1), respectively. X-ray crystallographic analysis of the pullulanase crystal showed that the crystal belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 70.568, b = 127.68, c = 189.25 angstroms. The crystal contains two molecules of pullulanase in the asymmetric unit, with a solvent content of 53.15%. The crystal diffracted to 2.1 angstroms resolution at a synchrotron and is suitable for structure determination.
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'''Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with maltose'''
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Overexpression, purification and preliminary X-ray analysis of pullulanase from Bacillus subtilis strain 168.,Malle D, Itoh T, Hashimoto W, Murata K, Utsumi S, Mikami B Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Apr 1;62(Pt, 4):381-4. Epub 2006 Mar 25. PMID:016582490<ref>PMID:016582490</ref>
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==Overview==
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The AmyX gene encoding pullulanase from the common spore-forming bacterium Bacillus subtilis strain 168 was cloned, overexpressed in Escherichia coli, purified and crystallized. The recombinant pullulanase was purified to homogeneity using ammonium sulfate precipitation, hydrophobic chromatography and anion-exchange chromatography, resulting in a specific activity of 24.10 U per milligram of protein. SDS-PAGE analysis showed that the molecular weight of the protein is approximately 81.0 kDa, which is similar to the calculated molecular weight, 81.1 kDa, from its translated cDNA sequence. The k(cat) and K(m) of the purified enzyme with pullulan as substrate were approximately 79 s(-1) and 1.284 mg ml(-1), respectively. X-ray crystallographic analysis of the pullulanase crystal showed that the crystal belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 70.568, b = 127.68, c = 189.25 angstroms. The crystal contains two molecules of pullulanase in the asymmetric unit, with a solvent content of 53.15%. The crystal diffracted to 2.1 angstroms resolution at a synchrotron and is suitable for structure determination.
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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2E9B is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E9B OCA].
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</div>
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<div class="pdbe-citations 2e9b" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Overexpression, purification and preliminary X-ray analysis of pullulanase from Bacillus subtilis strain 168., Malle D, Itoh T, Hashimoto W, Murata K, Utsumi S, Mikami B, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Apr 1;62(Pt, 4):381-4. Epub 2006 Mar 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16582490 16582490]
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*[[Amylase 3D structures|Amylase 3D structures]]
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[[Category: Bacillus subtilis]]
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== References ==
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[[Category: Pullulanase]]
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<references/>
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[[Category: Single protein]]
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__TOC__
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[[Category: Iwamoto, H.]]
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</StructureSection>
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[[Category: Katsuya, Y.]]
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[[Category: Large Structures]]
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[[Category: Malle, D.]]
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[[Category: Iwamoto H]]
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[[Category: Mikami, B.]]
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[[Category: Katsuya Y]]
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[[Category: Utsumi, S.]]
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[[Category: Malle D]]
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[[Category: Alpha-amylase-family maltose]]
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[[Category: Mikami B]]
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[[Category: Beta-alpha-barrel]]
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[[Category: Utsumi S]]
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[[Category: Hydrolase]]
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[[Category: Smultiple domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 02:10:42 2008''
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Current revision

Crystal structure of pullulanase type I from Bacillus subtilis str. 168 complexed with maltose

PDB ID 2e9b

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