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The Structural Basis of Erwinia rhapontici Isomaltulose Synthase
Sucrose isomerase NX-5 from Erwinia rhapontici efficiently catalyzes the isomerization of sucrose to isomaltulose (main product) and trehalulose (by-product). To investigate the molecular mechanism controlling sucrose isomer formation, we determined the crystal structures of native NX-5 and its muta...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3777934/ https://www.ncbi.nlm.nih.gov/pubmed/24069347 http://dx.doi.org/10.1371/journal.pone.0074788 |
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author | Xu, Zheng Li, Sha Li, Jie Li, Yan Feng, Xiaohai Wang, Renxiao Xu, Hong Zhou, Jiahai |
author_facet | Xu, Zheng Li, Sha Li, Jie Li, Yan Feng, Xiaohai Wang, Renxiao Xu, Hong Zhou, Jiahai |
author_sort | Xu, Zheng |
collection | PubMed |
description | Sucrose isomerase NX-5 from Erwinia rhapontici efficiently catalyzes the isomerization of sucrose to isomaltulose (main product) and trehalulose (by-product). To investigate the molecular mechanism controlling sucrose isomer formation, we determined the crystal structures of native NX-5 and its mutant complexes E295Q/sucrose and D241A/glucose at 1.70 Å, 1.70 Å and 2.00 Å, respectively. The overall structure and active site architecture of NX-5 resemble those of other reported sucrose isomerases. Strikingly, the substrate binding mode of NX-5 is also similar to that of trehalulose synthase from Pseudomonas mesoacidophila MX-45 (MutB). Detailed structural analysis revealed the catalytic RXDRX motif and the adjacent 10-residue loop of NX-5 and isomaltulose synthase PalI from Klebsiella sp. LX3 adopt a distinct orientation from those of trehalulose synthases. Mutations of the loop region of NX-5 resulted in significant changes of the product ratio between isomaltulose and trehalulose. The molecular dynamics simulation data supported the product specificity of NX-5 towards isomaltulose and the role of the loop(330-339) in NX-5 catalysis. This work should prove useful for the engineering of sucrose isomerase for industrial carbohydrate biotransformations. |
format | Online Article Text |
id | pubmed-3777934 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-37779342013-09-25 The Structural Basis of Erwinia rhapontici Isomaltulose Synthase Xu, Zheng Li, Sha Li, Jie Li, Yan Feng, Xiaohai Wang, Renxiao Xu, Hong Zhou, Jiahai PLoS One Research Article Sucrose isomerase NX-5 from Erwinia rhapontici efficiently catalyzes the isomerization of sucrose to isomaltulose (main product) and trehalulose (by-product). To investigate the molecular mechanism controlling sucrose isomer formation, we determined the crystal structures of native NX-5 and its mutant complexes E295Q/sucrose and D241A/glucose at 1.70 Å, 1.70 Å and 2.00 Å, respectively. The overall structure and active site architecture of NX-5 resemble those of other reported sucrose isomerases. Strikingly, the substrate binding mode of NX-5 is also similar to that of trehalulose synthase from Pseudomonas mesoacidophila MX-45 (MutB). Detailed structural analysis revealed the catalytic RXDRX motif and the adjacent 10-residue loop of NX-5 and isomaltulose synthase PalI from Klebsiella sp. LX3 adopt a distinct orientation from those of trehalulose synthases. Mutations of the loop region of NX-5 resulted in significant changes of the product ratio between isomaltulose and trehalulose. The molecular dynamics simulation data supported the product specificity of NX-5 towards isomaltulose and the role of the loop(330-339) in NX-5 catalysis. This work should prove useful for the engineering of sucrose isomerase for industrial carbohydrate biotransformations. Public Library of Science 2013-09-19 /pmc/articles/PMC3777934/ /pubmed/24069347 http://dx.doi.org/10.1371/journal.pone.0074788 Text en © 2013 Xu et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Xu, Zheng Li, Sha Li, Jie Li, Yan Feng, Xiaohai Wang, Renxiao Xu, Hong Zhou, Jiahai The Structural Basis of Erwinia rhapontici Isomaltulose Synthase |
title | The Structural Basis of Erwinia
rhapontici Isomaltulose Synthase |
title_full | The Structural Basis of Erwinia
rhapontici Isomaltulose Synthase |
title_fullStr | The Structural Basis of Erwinia
rhapontici Isomaltulose Synthase |
title_full_unstemmed | The Structural Basis of Erwinia
rhapontici Isomaltulose Synthase |
title_short | The Structural Basis of Erwinia
rhapontici Isomaltulose Synthase |
title_sort | structural basis of erwinia
rhapontici isomaltulose synthase |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3777934/ https://www.ncbi.nlm.nih.gov/pubmed/24069347 http://dx.doi.org/10.1371/journal.pone.0074788 |
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