Journal:Acta Cryst F:S2053230X23004430
From Proteopedia
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<scene name='96/967852/Homotetramer/3'>The ALDHSt homotetramer</scene> is a dimer of dimers (A/B and C/D) with crystallographic 222 symmetry. <scene name='96/967852/Monomer/1'>Structure of the monomer subunit</scene>. The cofactor-binding domain, catalytic domain and oligomerization domain are shown in green, cyan and magenta, respectively. NADP is shown as a yellow stick model. | <scene name='96/967852/Homotetramer/3'>The ALDHSt homotetramer</scene> is a dimer of dimers (A/B and C/D) with crystallographic 222 symmetry. <scene name='96/967852/Monomer/1'>Structure of the monomer subunit</scene>. The cofactor-binding domain, catalytic domain and oligomerization domain are shown in green, cyan and magenta, respectively. NADP is shown as a yellow stick model. | ||
| - | <scene name='96/967852/Binding_site/3'>Coenzyme NADP binding site</scene>. NADP and NADP-interacting residues are shown in ball-and-stick representation, water molecules are shown as red spheres. Hydrogen bonds are shown as dashed lines. <scene name='96/967852/Catalytic_residues/2'>The catalytic residues Asn142, Glu240, Cys274, Glu370 and Phe372</scene> (colored in deep pink). <scene name='96/967852/ | + | <scene name='96/967852/Binding_site/3'>Coenzyme NADP binding site</scene>. NADP and NADP-interacting residues are shown in ball-and-stick representation, water molecules are shown as red spheres. Hydrogen bonds are shown as dashed lines. <scene name='96/967852/Catalytic_residues/2'>The catalytic residues Asn142, Glu240, Cys274, Glu370 and Phe372</scene> (colored in deep pink). <scene name='96/967852/Asn142/1'>The conformation of the active-site residue Asn142 in ALDHSt</scene>. An omit F<sub>o</sub> - F<sub>c</sub> electron-density map for ligands was observed between the side chains of Asn142 and Cys274. This space appeared to be the binding-site cleft for the |
| + | substrate. Therefore, we propose the involvement of the amide group of the side chain | ||
| + | of Asn142 in an oxyanion hole to stabilize the reaction intermediate, as suggested previously. Arg88 and Phe143 were also observed near this site, but were not conserved in ALDH. | ||
<b>References</b><br> | <b>References</b><br> | ||
Revision as of 12:04, 31 May 2023
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