Journal:Acta Cryst D:S2059798318017047

The crystal structure of the N-acetylglucosamine 2-epimerase from Nostoc sp. KVJ10 reveals the true dimer

Marie-Josee Haglund Halsør, Ulli Rothweiler, Bjørn Altermark and Inger Lin Uttakleiv Ræder ^[1]

Molecular Tour
The crystal structure of the N-acetylglucosamine-2-epimerase from Nostoc sp. KVJ10 (nAGE10) was obtained at a resolution of 1.7 Å. The nAGE10 monomer is folds as a (α/α)₆-barrel in a manner similar to the previously published AGE structures. It is deposited in the PDB as 6f04. The previously reported dimer organization, which involved the “back-to-back” assembly of the monomers, could not be found within the nAGE10 crystal. However, a “front-to-front” dimer generated by symmetry is present in all AGE structures with better parameters than the back-to-back organization. The new AGE dimer places the putative ATP binding site(s) at the interface between the monomers with consequences regarding its role in AGE activity.

References

1. ↑ Halsor MJH, Rothweiler U, Altermark B, Raeder ILU. The crystal structure of the N-acetylglucosamine 2-epimerase from Nostoc sp. KVJ10 reveals the true dimer. Acta Crystallogr D Struct Biol. 2019 Jan 1;75(Pt 1):90-100. doi:, 10.1107/S2059798318017047. Epub 2019 Jan 8. PMID:30644848 doi:http://dx.doi.org/10.1107/S2059798318017047