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New page: left|200px<br /><applet load="1d3c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d3c, resolution 1.78Å" /> '''MICHAELIS COMPLEX OF...
 
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[[Image:1d3c.gif|left|200px]]<br /><applet load="1d3c" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1d3c, resolution 1.78&Aring;" />
'''MICHAELIS COMPLEX OF BACILLUS CIRCULANS STRAIN 251 CYCLODEXTRIN GLYCOSYLTRANSFERASE WITH GAMMA-CYCLODEXTRIN'''<br />


==Overview==
==MICHAELIS COMPLEX OF BACILLUS CIRCULANS STRAIN 251 CYCLODEXTRIN GLYCOSYLTRANSFERASE WITH GAMMA-CYCLODEXTRIN==
The enzyme cyclodextrin glycosyltransferase is closely related to, alpha-amylases but has the unique ability to produce cyclodextrins, (circular alpha(1--&gt;4)-linked glucoses) from starch. To characterize this, specificity we determined a 1.8-A structure of an E257Q/D229N mutant, cyclodextrin glycosyltransferase in complex with its product, gamma-cyclodextrin, which reveals for the first time how cyclodextrin is, competently bound. Across subsites -2, -1, and +1, the cyclodextrin ring, binds in a twisted mode similar to linear sugars, giving rise to, deformation of its circular symmetry. At subsites -3 and +2, the, cyclodextrin binds in a manner different from linear sugars. Sequence, comparisons and site-directed mutagenesis experiments support the, conclusion that subsites -3 and +2 confer the cyclization activity in, addition to subsite -6 and Tyr-195. On this basis, a role of the, individual residues during the cyclization reaction cycle is proposed.
<StructureSection load='1d3c' size='340' side='right'caption='[[1d3c]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1d3c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Niallia_circulans Niallia circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D3C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D3C 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]] 1.78&#8491;</td></tr>
<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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</scene>, <scene name='pdbligand=PRD_900042:gamma-cyclodextrin'>PRD_900042</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=1d3c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d3c OCA], [https://pdbe.org/1d3c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d3c RCSB], [https://www.ebi.ac.uk/pdbsum/1d3c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d3c ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CDGT2_NIACI CDGT2_NIACI]
== 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/d3/1d3c_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=1d3c ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The enzyme cyclodextrin glycosyltransferase is closely related to alpha-amylases but has the unique ability to produce cyclodextrins (circular alpha(1--&gt;4)-linked glucoses) from starch. To characterize this specificity we determined a 1.8-A structure of an E257Q/D229N mutant cyclodextrin glycosyltransferase in complex with its product gamma-cyclodextrin, which reveals for the first time how cyclodextrin is competently bound. Across subsites -2, -1, and +1, the cyclodextrin ring binds in a twisted mode similar to linear sugars, giving rise to deformation of its circular symmetry. At subsites -3 and +2, the cyclodextrin binds in a manner different from linear sugars. Sequence comparisons and site-directed mutagenesis experiments support the conclusion that subsites -3 and +2 confer the cyclization activity in addition to subsite -6 and Tyr-195. On this basis, a role of the individual residues during the cyclization reaction cycle is proposed.


==About this Structure==
The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-A resolution.,Uitdehaag JC, Kalk KH, van Der Veen BA, Dijkhuizen L, Dijkstra BW J Biol Chem. 1999 Dec 3;274(49):34868-76. PMID:10574960<ref>PMID:10574960</ref>
1D3C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans] with CA and MPD 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=1D3C OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-A resolution., Uitdehaag JC, Kalk KH, van Der Veen BA, Dijkhuizen L, Dijkstra BW, J Biol Chem. 1999 Dec 3;274(49):34868-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10574960 10574960]
</div>
[[Category: Bacillus circulans]]
<div class="pdbe-citations 1d3c" style="background-color:#fffaf0;"></div>
[[Category: Cyclomaltodextrin glucanotransferase]]
[[Category: Single protein]]
[[Category: Dijkhuizen, L.]]
[[Category: Dijkstra, B.W.]]
[[Category: Kalk, K.H.]]
[[Category: Uitdehaag, J.C.M.]]
[[Category: Veen, B.A.van.der.]]
[[Category: CA]]
[[Category: MPD]]
[[Category: alpha-amylase]]
[[Category: catalysis]]
[[Category: family 13 glycosyl hydrolase]]
[[Category: induced fit]]
[[Category: oligosaccharide]]
[[Category: product complex]]
[[Category: transglycosylation]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:58:57 2007''
==See Also==
*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Niallia circulans]]
[[Category: Dijkhuizen L]]
[[Category: Dijkstra BW]]
[[Category: Kalk KH]]
[[Category: Uitdehaag JCM]]
[[Category: Van der Veen BA]]

Latest revision as of 04:27, 17 October 2024

MICHAELIS COMPLEX OF BACILLUS CIRCULANS STRAIN 251 CYCLODEXTRIN GLYCOSYLTRANSFERASE WITH GAMMA-CYCLODEXTRIN

1d3c, resolution 1.78Å

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