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=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wms OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wms RCSB], [http://www.ebi.ac.uk/pdbsum/3wms PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wms FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wms OCA], [http://pdbe.org/3wms PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wms RCSB], [http://www.ebi.ac.uk/pdbsum/3wms PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wms ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3wms" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 17:50, 11 August 2016
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
Publication 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. References
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