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. is folds as a (α/α)6-barrel in a manner similar to the previously published AGE structures. The nAGE10 monomer shown from the side in a cartoon representation, it is colored in deepskyblue. Waters are shown as red, nonbonded spheres. Ethylene glycol molecules are represented as yellow sticks and the buried chloride ion as a green sphere. This crystal structure 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 is present in all AGE structures with better parameters than the back-to-back organization. The first nAGE10 monomer is colored in deepskyblue and the second nAGE10 monomer is in coral. The putative ATP-binding sites are colored in deeppink. 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
- ↑ 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
