1q6c

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[[Image:1q6c.gif|left|200px]]
 
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==Crystal Structure of Soybean Beta-Amylase Complexed with Maltose==
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The line below this paragraph, containing "STRUCTURE_1q6c", creates the "Structure Box" on the page.
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<StructureSection load='1q6c' size='340' side='right'caption='[[1q6c]], [[Resolution|resolution]] 1.86&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'>[[1q6c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q6C 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]] 1.86&#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=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1q6c| PDB=1q6c | 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=1q6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q6c OCA], [https://pdbe.org/1q6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q6c RCSB], [https://www.ebi.ac.uk/pdbsum/1q6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q6c ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMYB_SOYBN AMYB_SOYBN]
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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/q6/1q6c_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=1q6c ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure of Soybean Beta-Amylase Complexed with Maltose'''
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==See Also==
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*[[Amylase 3D structures|Amylase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Comparison of the architecture around the active site of soybean beta-amylase and Bacillus cereus beta-amylase showed that the hydrogen bond networks (Glu380-(Lys295-Met51) and Glu380-Asn340-Glu178) in soybean beta-amylase around the base catalytic residue, Glu380, seem to contribute to the lower pH optimum of soybean beta-amylase. To convert the pH optimum of soybean beta-amylase (pH 5.4) to that of the bacterial type enzyme (pH 6.7), three mutants of soybean beta-amylase, M51T, E178Y, and N340T, were constructed such that the hydrogen bond networks were removed by site-directed mutagenesis. The kinetic analysis showed that the pH optimum of all mutants shifted dramatically to a neutral pH (range, from 5.4 to 6.0-6.6). The Km values of the mutants were almost the same as that of soybean beta-amylase except in the case of M51T, while the Vmax values of all mutants were low compared with that of soybean beta-amylase. The crystal structure analysis of the wild type-maltose and mutant-maltose complexes showed that the direct hydrogen bond between Glu380 and Asn340 was completely disrupted in the mutants M51T, E178Y, and N340T. In the case of M51T, the hydrogen bond between Glu380 and Lys295 was also disrupted. These results indicated that the reduced pKa value of Glu380 is stabilized by the hydrogen bond network and is responsible for the lower pH optimum of soybean beta-amylase compared with that of the bacterial beta-amylase.
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==About this Structure==
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1Q6C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q6C OCA].
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==Reference==
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Structural and enzymatic analysis of soybean beta-amylase mutants with increased pH optimum., Hirata A, Adachi M, Sekine A, Kang YN, Utsumi S, Mikami B, J Biol Chem. 2004 Feb 20;279(8):7287-95. Epub 2003 Nov 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14638688 14638688]
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[[Category: Beta-amylase]]
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[[Category: Glycine max]]
[[Category: Glycine max]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Adachi, M.]]
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[[Category: Adachi M]]
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[[Category: Hirata, A.]]
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[[Category: Hirata A]]
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[[Category: Kang, Y N.]]
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[[Category: Kang YN]]
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[[Category: Mikami, B.]]
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[[Category: Mikami B]]
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[[Category: Sekine, A.]]
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[[Category: Sekine A]]
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[[Category: Utsumi, S.]]
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[[Category: Utsumi S]]
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[[Category: Beta-alpha-barrel]]
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[[Category: Beta-amylase]]
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[[Category: Maltose complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:55:27 2008''
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Current revision

Crystal Structure of Soybean Beta-Amylase Complexed with Maltose

PDB ID 1q6c

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