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New page: left|200px<br /><applet load="1ded" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ded, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1ded.gif|left|200px]]<br /><applet load="1ded" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ded, resolution 2.0&Aring;" />
'''CRYSTAL STRUCTURE OF ALKALOPHILIC ASPARAGINE 233-REPLACED CYCLODEXTRIN GLUCANOTRANSFERASE COMPLEXED WITH AN INHIBITOR, ACARBOSE, AT 2.0 A RESOLUTION'''<br />


==Overview==
==CRYSTAL STRUCTURE OF ALKALOPHILIC ASPARAGINE 233-REPLACED CYCLODEXTRIN GLUCANOTRANSFERASE COMPLEXED WITH AN INHIBITOR, ACARBOSE, AT 2.0 A RESOLUTION==
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.
<StructureSection load='1ded' size='340' side='right'caption='[[1ded]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<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>
<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>
== Function ==
[https://www.uniprot.org/uniprot/CDGT_BACS0 CDGT_BACS0]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/de/1ded_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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="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.


==About this Structure==
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>
1DED is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.] with ACR and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cyclomaltodextrin_glucanotransferase Cyclomaltodextrin glucanotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.19 2.4.1.19] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DED OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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 (Tokyo). 2000 Mar;127(3):383-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10731709 10731709]
</div>
[[Category: Bacillus sp.]]
<div class="pdbe-citations 1ded" style="background-color:#fffaf0;"></div>
[[Category: Cyclomaltodextrin glucanotransferase]]
[[Category: Single protein]]
[[Category: Haga, K.]]
[[Category: Harata, K.]]
[[Category: Ishii, N.]]
[[Category: Yamane, K.]]
[[Category: ACR]]
[[Category: CA]]
[[Category: acarbose]]
[[Category: cgtase]]
[[Category: cyclodextrin glucanotransferase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:12:59 2007''
==See Also==
*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus sp. 1011]]
[[Category: Large Structures]]
[[Category: Haga K]]
[[Category: Harata K]]
[[Category: Ishii N]]
[[Category: Yamane K]]

Latest revision as of 07:13, 9 October 2024

CRYSTAL STRUCTURE OF ALKALOPHILIC ASPARAGINE 233-REPLACED CYCLODEXTRIN GLUCANOTRANSFERASE COMPLEXED WITH AN INHIBITOR, ACARBOSE, AT 2.0 A RESOLUTION

1ded, resolution 2.00Å

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