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The crystal structure of the N-acetylglucosamine 2-epimerase from Nostoc sp. KVJ10 reveals the true dimer
N-Acetylglucosamine 2-epimerases (AGEs) catalyze the interconversion of N-acetylglucosamine and N-acetylmannosamine. They can be used to perform the first step in the synthesis of sialic acid from N-acetylglucosamine, which makes the need for efficient AGEs a priority. This study presents the struct...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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International Union of Crystallography
2019
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6333288/ https://www.ncbi.nlm.nih.gov/pubmed/30644848 http://dx.doi.org/10.1107/S2059798318017047 |
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author | Halsør, Marie-Josée Haglund Rothweiler, Ulli Altermark, Bjørn Raeder, Inger Lin Uttakleiv |
author_facet | Halsør, Marie-Josée Haglund Rothweiler, Ulli Altermark, Bjørn Raeder, Inger Lin Uttakleiv |
author_sort | Halsør, Marie-Josée Haglund |
collection | PubMed |
description | N-Acetylglucosamine 2-epimerases (AGEs) catalyze the interconversion of N-acetylglucosamine and N-acetylmannosamine. They can be used to perform the first step in the synthesis of sialic acid from N-acetylglucosamine, which makes the need for efficient AGEs a priority. This study presents the structure of the AGE from Nostoc sp. KVJ10 collected in northern Norway, referred to as nAGE10. It is the third AGE structure to be published to date, and the first one in space group P4(2)2(1)2. The nAGE10 monomer folds as an (α/α)(6) barrel in a similar manner to that of the previously published AGEs, but the crystal did not contain the dimers that have previously been reported. The previously proposed ‘back-to-back’ assembly involved the face of the AGE monomer where the barrel helices are connected by small loops. Instead, a ‘front-to-front’ dimer was found in nAGE10 involving the long loops that connect the barrel helices at this end. This assembly is also present in the other AGE structures, but was attributed to crystal packing, even though the ‘front’ interface areas are larger and are more conserved than the ‘back’ interface areas. In addition, the front-to-front association allows a better explanation of the previously reported observations considering surface cysteines. Together, these results indicate that the ‘front-to-front’ dimer is the most probable biological assembly for AGEs. |
format | Online Article Text |
id | pubmed-6333288 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-63332882019-02-01 The crystal structure of the N-acetylglucosamine 2-epimerase from Nostoc sp. KVJ10 reveals the true dimer Halsør, Marie-Josée Haglund Rothweiler, Ulli Altermark, Bjørn Raeder, Inger Lin Uttakleiv Acta Crystallogr D Struct Biol Research Papers N-Acetylglucosamine 2-epimerases (AGEs) catalyze the interconversion of N-acetylglucosamine and N-acetylmannosamine. They can be used to perform the first step in the synthesis of sialic acid from N-acetylglucosamine, which makes the need for efficient AGEs a priority. This study presents the structure of the AGE from Nostoc sp. KVJ10 collected in northern Norway, referred to as nAGE10. It is the third AGE structure to be published to date, and the first one in space group P4(2)2(1)2. The nAGE10 monomer folds as an (α/α)(6) barrel in a similar manner to that of the previously published AGEs, but the crystal did not contain the dimers that have previously been reported. The previously proposed ‘back-to-back’ assembly involved the face of the AGE monomer where the barrel helices are connected by small loops. Instead, a ‘front-to-front’ dimer was found in nAGE10 involving the long loops that connect the barrel helices at this end. This assembly is also present in the other AGE structures, but was attributed to crystal packing, even though the ‘front’ interface areas are larger and are more conserved than the ‘back’ interface areas. In addition, the front-to-front association allows a better explanation of the previously reported observations considering surface cysteines. Together, these results indicate that the ‘front-to-front’ dimer is the most probable biological assembly for AGEs. International Union of Crystallography 2019-01-08 /pmc/articles/PMC6333288/ /pubmed/30644848 http://dx.doi.org/10.1107/S2059798318017047 Text en © Halsør et al. 2019 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited.http://creativecommons.org/licenses/by/2.0/uk/ |
spellingShingle | Research Papers Halsør, Marie-Josée Haglund Rothweiler, Ulli Altermark, Bjørn Raeder, Inger Lin Uttakleiv The crystal structure of the N-acetylglucosamine 2-epimerase from Nostoc sp. KVJ10 reveals the true dimer |
title | The crystal structure of the N-acetylglucosamine 2-epimerase from Nostoc sp. KVJ10 reveals the true dimer |
title_full | The crystal structure of the N-acetylglucosamine 2-epimerase from Nostoc sp. KVJ10 reveals the true dimer |
title_fullStr | The crystal structure of the N-acetylglucosamine 2-epimerase from Nostoc sp. KVJ10 reveals the true dimer |
title_full_unstemmed | The crystal structure of the N-acetylglucosamine 2-epimerase from Nostoc sp. KVJ10 reveals the true dimer |
title_short | The crystal structure of the N-acetylglucosamine 2-epimerase from Nostoc sp. KVJ10 reveals the true dimer |
title_sort | crystal structure of the n-acetylglucosamine 2-epimerase from nostoc sp. kvj10 reveals the true dimer |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6333288/ https://www.ncbi.nlm.nih.gov/pubmed/30644848 http://dx.doi.org/10.1107/S2059798318017047 |
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