3wms: Difference between revisions
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==The crystal structure of Y195I mutant alpha-cyclodextrin glycosyltransferase from Paenibacillus macerans== | ==The crystal structure of Y195I mutant alpha-cyclodextrin glycosyltransferase from Paenibacillus macerans== | ||
<StructureSection load='3wms' size='340' side='right' caption='[[3wms]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='3wms' size='340' side='right'caption='[[3wms]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3wms]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WMS OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[3wms]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenibacillus_macerans Paenibacillus macerans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WMS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WMS FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wms OCA], [https://pdbe.org/3wms PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wms RCSB], [https://www.ebi.ac.uk/pdbsum/3wms PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wms ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/CDGT1_PAEMA CDGT1_PAEMA] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 3wms" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3wms" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Glycosyltransferase 3D structures|Glycosyltransferase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Chao | [[Category: Paenibacillus macerans]] | ||
[[Category: Hou | [[Category: Chao YP]] | ||
[[Category: Li | [[Category: Hou YJ]] | ||
[[Category: Qian | [[Category: Li DF]] | ||
[[Category: Xie | [[Category: Qian SJ]] | ||
[[Category: Yue | [[Category: Xie T]] | ||
[[Category: Yue Y]] | |||
Latest revision as of 16:15, 8 November 2023
The crystal structure of Y195I mutant alpha-cyclodextrin glycosyltransferase from Paenibacillus maceransThe crystal structure of Y195I mutant alpha-cyclodextrin glycosyltransferase from Paenibacillus macerans
Structural highlights
FunctionPublication Abstract from PubMedCyclodextrin glycosyltransferase (EC 2.4.1.19) (CGTase) is an extracellular bacterial enzyme which has the unique capability of forming cyclodextrins from starch. Our previous investigation revealed that a mutant Y195I alpha-CGTase drastically altered the cyclodextrin specificity by switching toward the synthesis of both beta- and gamma-CDs (Xie et al., 2013a,b). In this study, we determined one X-ray structure of the mutant Y195I alpha-CGTase at 2.3A. The overall structure was similar to that of the typical beta-CGTase from Bacillus circulans 251, with minor difference in flexible domains since they showed about 70% homogeneity of amino acid sequences. The central site with isoleucine tended to be more flexible than tyrosine thus made the sugar chain, during the cyclization process, form a larger cyclodextrin like beta- and gamma-CDs surrounding the central site instead of alpha-CD. Superposition of the structure of Y195I alpha-CGTase with those of beta-CGTase and gamma-CGTase showed that residues Lys232, Lys89 and Arg177 at subsites +2, -3 and -7 could form smaller substrate binding cavity. In summary, the crystal structure revealed that moderate increase of mobility of the central site resulted in the switched product specificity from alpha-CD to beta- and gamma-CDs of the mutant Y195I alpha-CGTase. The space differences alongside the active domain may be another factor that impacts the product specificity of the CGTase. Structural basis of a mutant Y195I alpha-cyclodextrin glycosyltransferase with switched product specificity from alpha-cyclodextrin to beta-/gamma-cyclodextrin.,Xie T, Hou Y, Li D, Yue Y, Qian S, Chao Y J Biotechnol. 2014 Jul 20;182-183:92-6. doi: 10.1016/j.jbiotec.2014.03.014. Epub , 2014 Mar 15. PMID:24637377[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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