5cgt: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (8 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
< | ==MALTOTRIOSE COMPLEX OF PRECONDITIONED CYCLODEXTRIN GLYCOSYLTRANSFERASE MUTANT== | ||
<StructureSection load='5cgt' size='340' side='right'caption='[[5cgt]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5cgt]] 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=5CGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CGT 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]] 2.5Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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_900018:beta-maltose'>PRD_900018</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=5cgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cgt OCA], [https://pdbe.org/5cgt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cgt RCSB], [https://www.ebi.ac.uk/pdbsum/5cgt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cgt 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/5cgt_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=5cgt 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5cgt" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[Category: Niallia circulans]] | |||
[[Category: Parsiegla G]] | |||
== | [[Category: Schulz GE]] | ||
[[Category: | |||
[[Category: | |||
[[Category: Parsiegla | |||
[[Category: Schulz | |||
Latest revision as of 13:36, 30 October 2024
MALTOTRIOSE COMPLEX OF PRECONDITIONED CYCLODEXTRIN GLYCOSYLTRANSFERASE MUTANTMALTOTRIOSE COMPLEX OF PRECONDITIONED CYCLODEXTRIN GLYCOSYLTRANSFERASE MUTANT
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBacterial 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 AlsoReferences |
| ||||||||||||||||||