Journal:Acta Cryst D:S2059798318017047
From Proteopedia
(Difference between revisions)

Line 7: | Line 7: | ||
<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
The crystal structure of the N-acetylglucosamine-2-epimerase from ''Nostoc'' sp. KVJ10 (nAGE10) was obtained at a resolution of 1.7 Å. <scene name='80/801848/Cv/3'>The nAGE10 monomer</scene> is folds as a (α/α)<sub>6</sub>-barrel in a manner similar to the previously published AGE structures. <span style="color:deepskyblue;background-color:black;font-weight:bold;">The nAGE10 monomer shown from the side in a cartoon representation, it is colored in deepskyblue</span>. <span style="color:red;background-color:black;font-weight:bold;">Waters are shown as red, nonbonded spheres</span>. <span style="color:yellow;background-color:black;font-weight:bold;">Ethylene glycol molecules are represented as yellow sticks</span> and the buried <span style="color:lime;background-color:black;font-weight:bold;">chloride ion as a green sphere</span>. This crystal structure is deposited in the PDB as [[6f04]]. | The crystal structure of the N-acetylglucosamine-2-epimerase from ''Nostoc'' sp. KVJ10 (nAGE10) was obtained at a resolution of 1.7 Å. <scene name='80/801848/Cv/3'>The nAGE10 monomer</scene> is folds as a (α/α)<sub>6</sub>-barrel in a manner similar to the previously published AGE structures. <span style="color:deepskyblue;background-color:black;font-weight:bold;">The nAGE10 monomer shown from the side in a cartoon representation, it is colored in deepskyblue</span>. <span style="color:red;background-color:black;font-weight:bold;">Waters are shown as red, nonbonded spheres</span>. <span style="color:yellow;background-color:black;font-weight:bold;">Ethylene glycol molecules are represented as yellow sticks</span> and the buried <span style="color:lime;background-color:black;font-weight:bold;">chloride ion as a green sphere</span>. 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 “front-to-front” dimer generated by symmetry is present in all AGE structures with better parameters than the back-to-back organization. | + | 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 <scene name='80/801848/Cv/4'>“front-to-front” dimer generated by symmetry</scene> 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. | 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. | ||
Revision as of 13:42, 5 December 2018
http://proteopedia.org/w/Journal:Acta_Cryst_D:S2059798318017047
|
This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.