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1qpk

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[[Image:1qpk.jpg|left|200px]]<br /><applet load="1qpk" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qpk, resolution 2.0&Aring;" />
 
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'''MUTANT (D193G) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX WITH MALTOTETRAOSE'''<br />
 
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==Overview==
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==MUTANT (D193G) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX WITH MALTOTETRAOSE==
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The crystal structures of the four product-complexed single mutants of the catalytic residues of Pseudomonas stutzeri maltotetraose-forming alpha-amylase, E219G, D193N, D193G and D294N, have been determined. Possible roles of the catalytic residues Glu219, Asp193 and Asp294 have been discussed by comparing the structures among the previously determined complexed mutant E219Q and the present mutant enzymes. The results suggested that Asp193 predominantly works as the base catalyst (nucleophile), whose side chain atom lies in close proximity to the C1-atom of Glc4, being involved in the intermediate formation in the hydrolysis reaction. While Asp294 works for tightly binding the substrate to give a twisted and a deformed conformation of the glucose ring at position -1 (Glc4). The hydrogen bond between the side chain atom of Glu219 and the O1-atom of Glc4, that implies the possibility of interaction via hydrogen, consistently present throughout these analyses, supports the generally accepted role of this residue as the acid catalyst (proton donor).
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<StructureSection load='1qpk' size='340' side='right'caption='[[1qpk]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1qpk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QPK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QPK FirstGlance]. <br>
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1QPK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_stutzeri Pseudomonas stutzeri] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=MTT:'>MTT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QPK OCA].
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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&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900010:alpha-maltotetraose'>PRD_900010</scene></td></tr>
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==Reference==
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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=1qpk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qpk OCA], [https://pdbe.org/1qpk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qpk RCSB], [https://www.ebi.ac.uk/pdbsum/1qpk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qpk ProSAT]</span></td></tr>
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Roles of catalytic residues in alpha-amylases as evidenced by the structures of the product-complexed mutants of a maltotetraose-forming amylase., Hasegawa K, Kubota M, Matsuura Y, Protein Eng. 1999 Oct;12(10):819-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10556241 10556241]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMT4_STUST AMT4_STUST]
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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/qp/1qpk_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=1qpk ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Pseudomonas stutzeri]]
[[Category: Pseudomonas stutzeri]]
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[[Category: Single protein]]
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[[Category: Hasegawa K]]
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[[Category: Hasegawa, K.]]
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[[Category: Katsube Y]]
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[[Category: Katsube, Y.]]
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[[Category: Kubota M]]
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[[Category: Kubota, M.]]
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[[Category: Matsuura Y]]
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[[Category: Matsuura, Y.]]
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[[Category: Yoshioka Y]]
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[[Category: Yoshioka, Y.]]
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[[Category: CA]]
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[[Category: MTT]]
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[[Category: beta-alpha-barrels]]
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[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:42:23 2008''
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Current revision

MUTANT (D193G) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX WITH MALTOTETRAOSE

PDB ID 1qpk

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