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1jdc

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(New page: 200px<br /><applet load="1jdc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jdc, resolution 1.9&Aring;" /> '''MUTANT (E219Q) MALTOT...)
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[[Image:1jdc.gif|left|200px]]<br /><applet load="1jdc" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1jdc, resolution 1.9&Aring;" />
 
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'''MUTANT (E219Q) MALTOTETRAOSE-FORMING EXO-AMYLASE COCRYSTALLIZED WITH MALTOTETRAOSE (CRYSTAL TYPE 1)'''<br />
 
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==Overview==
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==MUTANT (E219Q) MALTOTETRAOSE-FORMING EXO-AMYLASE COCRYSTALLIZED WITH MALTOTETRAOSE (CRYSTAL TYPE 1)==
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The three-dimensional structures of the catalytic residue Glu219--&gt;Gln, mutant of Pseudomonas stutzeri maltotetraose-forming exo-alpha-amylase, and its complex with carbohydrate obtained by cocrystallization with, maltopentaose were determined. Two crystal forms were obtained for the, complexed enzyme, and a bound maltotetraose was found in each. The, structures were analyzed at 2.2 A and 1.9 A resolution, respectively for, the uncomplexed and complexed mutant. These structures were compared with, the wild-type enzyme structure. In the complexed crystals, the, maltotetraose was firmly bound, extensively interacting with the amino, acid environments in the active cleft. The non-reducing end glucose unit, was hydrogen bonded to the side-chain of Asp160 and the main-chain, nitrogen of Gly158, which seem to be predominantly required for the, recognition of the non-reducing end of the substrate that determines the, exo-wise degradation of this enzyme. The reducing end glucose unit of, bound maltotetraose showed clear deformation, adopting a half-chair, conformation with extensive hydrogen bonds to surrounding polypeptides., The C1-atom of this deformed glucose unit lies very close to Asp193OD1, with a distance of 2.6 A. The catalytic residue Asp294 is firmly, hydrogen-bonded to the O2 and O3-hydroxyl groups of the deformed reducing, end glucose unit. Upon binding of the carbohydrate, small but significant, induced fits were observed in the regions of Asp294, Phe156, Ile157, and, Asp160. Possible roles of the three catalytic residues are also discussed.
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<StructureSection load='1jdc' size='340' side='right'caption='[[1jdc]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1jdc]] 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=1JDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JDC FirstGlance]. <br>
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1JDC 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 CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glucan_1,4-alpha-maltotetraohydrolase Glucan 1,4-alpha-maltotetraohydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.60 3.2.1.60] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JDC 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]] 1.9&#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=1jdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jdc OCA], [https://pdbe.org/1jdc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jdc RCSB], [https://www.ebi.ac.uk/pdbsum/1jdc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jdc ProSAT]</span></td></tr>
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Crystal structures of a mutant maltotetraose-forming exo-amylase cocrystallized with maltopentaose., Yoshioka Y, Hasegawa K, Matsuura Y, Katsube Y, Kubota M, J Mol Biol. 1997 Aug 29;271(4):619-28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9281429 9281429]
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</table>
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[[Category: Glucan 1,4-alpha-maltotetraohydrolase]]
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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/jd/1jdc_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=1jdc 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: hydrolase]]
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[[Category: maltotetraose-forming exo amylase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:07:59 2007''
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Current revision

MUTANT (E219Q) MALTOTETRAOSE-FORMING EXO-AMYLASE COCRYSTALLIZED WITH MALTOTETRAOSE (CRYSTAL TYPE 1)

PDB ID 1jdc

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