6cgt: Difference between revisions

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<StructureSection load='6cgt' size='340' side='right'caption='[[6cgt]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='6cgt' size='340' side='right'caption='[[6cgt]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6cgt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_24 Atcc 24]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CGT FirstGlance]. <br>
<table><tr><td colspan='2'>[[6cgt]] 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=6CGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CGT FirstGlance]. <br>
</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=OPG:OXIRANPSEUDOGLUCOSE'>OPG</scene>, <scene name='pdbligand=DAG:4,6-DIDEOXY-4-AMINO-BETA-D-GLUCOPYRANOSIDE'>DAG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cyclomaltodextrin_glucanotransferase Cyclomaltodextrin glucanotransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.19 2.4.1.19] </span></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=DAG:4,6-DIDEOXY-4-AMINO-BETA-D-GLUCOPYRANOSIDE'>DAG</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=OPG:OXIRANPSEUDOGLUCOSE'>OPG</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=6cgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cgt OCA], [https://pdbe.org/6cgt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cgt RCSB], [https://www.ebi.ac.uk/pdbsum/6cgt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cgt 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=6cgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cgt OCA], [https://pdbe.org/6cgt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cgt RCSB], [https://www.ebi.ac.uk/pdbsum/6cgt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cgt ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CDGT1_NIACI CDGT1_NIACI]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cg/6cgt_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cg/6cgt_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 24]]
[[Category: Cyclomaltodextrin glucanotransferase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Parsiegla, G]]
[[Category: Niallia circulans]]
[[Category: Schulz, G E]]
[[Category: Parsiegla G]]
[[Category: Cyclodextrin]]
[[Category: Schulz GE]]
[[Category: Glycosyltransferase]]
[[Category: Starch degradation]]

Latest revision as of 10:51, 17 October 2024

HOXA COMPLEX OF CYCLODEXTRIN GLYCOSYLTRANSFERASE MUTANTHOXA COMPLEX OF CYCLODEXTRIN GLYCOSYLTRANSFERASE MUTANT

Structural highlights

6cgt is a 1 chain structure with sequence from Niallia circulans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CDGT1_NIACI

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Bacterial cyclodextrin glycosyltransferases use starch to produce cyclic maltooligosaccharides (cyclodextrins) which are of interest in various applications. The cyclization reaction gives rise to a spectrum of ring sizes consisting of predominantly six to eight glucosyl units. Using the enzyme from Bacillus circulans strain no. 8, binding studies have been performed with several substrates and analogues. The observed binding modes differ in detail, but agree in general with data on homologous enzymes. Based on these binding studies, two mutations were designed that changed the production spectrum from the predominant product beta-cyclodextrin of the wild-type enzyme towards gamma-cyclodextrin, which is of practical interest because it is rare and can encapsulate larger nonpolar compounds.

Substrate binding to a cyclodextrin glycosyltransferase and mutations increasing the gamma-cyclodextrin production.,Parsiegla G, Schmidt AK, Schulz GE Eur J Biochem. 1998 Aug 1;255(3):710-7. PMID:9738912[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Parsiegla G, Schmidt AK, Schulz GE. Substrate binding to a cyclodextrin glycosyltransferase and mutations increasing the gamma-cyclodextrin production. Eur J Biochem. 1998 Aug 1;255(3):710-7. PMID:9738912

6cgt, resolution 2.60Å

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OCA