6cgt: Difference between revisions

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-[[Image:6cgt.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_6cgt", creates the "Structure Box" on the page.
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-or leave the SCENE parameter empty for the default display.
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-{{STRUCTURE_6cgt|  PDB=6cgt  |  SCENE=  }}
-'''HOXA COMPLEX OF CYCLODEXTRIN GLYCOSYLTRANSFERASE MUTANT'''
+==HOXA COMPLEX OF CYCLODEXTRIN GLYCOSYLTRANSFERASE MUTANT==
+<StructureSection load='6cgt' size='340' side='right'caption='[[6cgt]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<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='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='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>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CDGT1_NIACI CDGT1_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/cg/6cgt_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=6cgt ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-==Overview==
+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<ref>PMID:9738912</ref>
-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.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-CGT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CGT OCA].
+</div>
+<div class="pdbe-citations 6cgt" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/9738912 9738912]
+*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]]
-[[Category: Bacillus circulans]]
+== References ==
-[[Category: Cyclomaltodextrin glucanotransferase]]
+<references/>
-[[Category: Single protein]]
+__TOC__
-[[Category: Parsiegla, G.]]
+</StructureSection>
-[[Category: Schulz, G E.]]
+[[Category: Large Structures]]
-[[Category: Cyclodextrin]]
+[[Category: Niallia circulans]]
-[[Category: Glycosyltransferase]]
+[[Category: Parsiegla G]]
-[[Category: Starch degradation]]
+[[Category: Schulz GE]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:39:34 2008''