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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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Autores principales: Halsør, Marie-Josée Haglund, Rothweiler, Ulli, Altermark, Bjørn, Raeder, Inger Lin Uttakleiv
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2019
Materias:
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.
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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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