Journal:Acta Cryst D:S2059798318017047

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http://proteopedia.org/w/Journal:Acta_Cryst_D:S2059798318017047
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<StructureSection load='' size='450' side='right' scene='80/801848/Cv/1' caption=''>
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===The crystal structure of the N-acetylglucosamine 2-epimerase from ''Nostoc sp.'' KVJ10 reveals the true dimer===
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<StructureSection load='' size='450' side='right' scene='underdevelopment' caption=''>
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===The crystal structure of the N-acetylglucosamine 2-epimerase from Nostoc sp. KVJ10 reveals the true dimer===
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<big>Marie-Josee Haglund Halsør, Ulli Rothweiler, Bjørn Altermark and Inger Lin Uttakleiv Ræder</big> <ref>doi 10.1107/S2059798318017047</ref>
<big>Marie-Josee Haglund Halsør, Ulli Rothweiler, Bjørn Altermark and Inger Lin Uttakleiv Ræder</big> <ref>doi 10.1107/S2059798318017047</ref>
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<b>Molecular Tour</b><br>
<b>Molecular Tour</b><br>
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The crystal structure of the N-acetylglucosamine-2-epimerase from Nostoc sp. KVJ10 (nAGE10) was obtained at a resolution of 1.7ֳ…. The nAGE10 monomer is folds as a (־±/ ־±)6-barrel in a manner similar to the previously published AGE structures. It is deposited in the PDB as 6F04.
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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]].
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The previously reported dimer organization, which involved the ג€œbacksג€ of the monomers, could not be found within the nAGE10 crystal. However, a ג€œfront-to-frontג€ dimer generated by symmetry is present in all AGE structures with better parameters than the back-to-back organization.
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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. <span style="color:deepskyblue;background-color:black;font-weight:bold;">The first nAGE10 monomer is colored in deepskyblue</span> and <span style="color:coral;background-color:black;font-weight:bold;">the second nAGE10 monomer is in coral</span>. The new AGE dimer places <scene name='80/801848/Cv/5'>the putative ATP binding site(s)</scene> (<span style="color:deeppink;background-color:black;font-weight:bold;">colored in deeppink</span>) at the interface between the monomers with consequences regarding its role in AGE activity.
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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.
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'''PDB reference:''' N-acetylglucosamine-2-epimerase [[6f04]].
<b>References</b><br>
<b>References</b><br>

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