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1ded
From Proteopedia
(Difference between revisions)
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<StructureSection load='1ded' size='340' side='right'caption='[[1ded]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1ded' size='340' side='right'caption='[[1ded]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1ded]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1ded]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._1011 Bacillus sp. 1011]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DED FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AC1:6-METHYL-5-(4,5,6-TRIHYDROXY-3-HYDROXYMETHYL-CYCLOHEX-2-ENYLAMINO)-TETRAHYDRO-PYRAN-2,3,4-TRIOL'>AC1</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=PRD_900022:beta-acarbose'>PRD_900022</scene></td></tr> |
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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=1ded FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ded OCA], [https://pdbe.org/1ded PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ded RCSB], [https://www.ebi.ac.uk/pdbsum/1ded PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ded ProSAT]</span></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=1ded FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ded OCA], [https://pdbe.org/1ded PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ded RCSB], [https://www.ebi.ac.uk/pdbsum/1ded PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ded ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CDGT_BACS0 CDGT_BACS0] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1ded ConSurf]. | </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=1ded ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The product specificity of cyclodextrin glucanotransferase (CGTase) from alkalophilic Bacillus sp. #1011 is improved to near-uniformity by mutation of histidine-233 to asparagine. Asparagine 233-replaced CGTase (H233N-CGTase) no longer produces alpha-cyclodextrin, while the wild-type CGTase from the same bacterium produces a mixture of predominantly alpha-, beta-, and gamma-cyclodextrins, catalyzing the conversion of starch into cyclic or linear alpha-1,4-linked glucopyranosyl chains. In order to better understand the protein engineering of H233N-CGTase, the crystal structure of the mutant enzyme complexed with a maltotetraose analog, acarbose, was determined at 2.0 A resolution with a final crystallographic R value of 0.163 for all data. Taking a close look at the active site cleft in which the acarbose molecule is bound, the most probable reason for the improved specificity of H233N-CGTase is the removal of interactions needed to form a compact ring like a-cyclodextrin. | ||
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| - | Crystal structure of alkalophilic asparagine 233-replaced cyclodextrin glucanotransferase complexed with an inhibitor, acarbose, at 2.0 A resolution.,Ishii N, Haga K, Yamane K, Harata K J Biochem. 2000 Mar;127(3):383-91. PMID:10731709<ref>PMID:10731709</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1ded" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]] | *[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bacillus sp. 1011]] |
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Haga | + | [[Category: Haga K]] |
| - | [[Category: Harata | + | [[Category: Harata K]] |
| - | [[Category: Ishii | + | [[Category: Ishii N]] |
| - | [[Category: Yamane | + | [[Category: Yamane K]] |
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Current revision
CRYSTAL STRUCTURE OF ALKALOPHILIC ASPARAGINE 233-REPLACED CYCLODEXTRIN GLUCANOTRANSFERASE COMPLEXED WITH AN INHIBITOR, ACARBOSE, AT 2.0 A RESOLUTION
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