Journal:MicroPubl Biol:000570

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*<scene name='91/913474/Cv/6'>1st view</scene>.
*<scene name='91/913474/Cv/6'>1st view</scene>.
*<scene name='91/913474/Cv/9'>2nd view. Rotated ~ 90° clockwise around the vertical axis, respective to the orientation shown at 1st view</scene>.
*<scene name='91/913474/Cv/9'>2nd view. Rotated ~ 90° clockwise around the vertical axis, respective to the orientation shown at 1st view</scene>.
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*<scene name='91/913474/Cv/8'>3rd view. after ~90° rotation</scene>.
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*<scene name='91/913474/Cv/8'>3rd view. Rotated ~ 90° clockwise around the horizontal axis, respective to the orientation shown at 1st view</scene>.
The crystallographic model (PDB [[6pup]]), electrostatic potential:
The crystallographic model (PDB [[6pup]]), electrostatic potential:
*<scene name='91/913474/Cv/10'>1st view</scene>.
*<scene name='91/913474/Cv/10'>1st view</scene>.
*<scene name='91/913474/Cv/11'>2nd view. Rotated ~ 90° clockwise around the vertical axis, respective to the orientation shown at 1st view</scene>.
*<scene name='91/913474/Cv/11'>2nd view. Rotated ~ 90° clockwise around the vertical axis, respective to the orientation shown at 1st view</scene>.
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*<scene name='91/913474/Cv/12'>3rd view after ~90° rotation</scene>.
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*<scene name='91/913474/Cv/12'>3rd view. Rotated ~ 90° clockwise around the horizontal axis, respective to the orientation shown at 1st view</scene>.
The crystallographic model (PDB [[6pup]]) contains two Mn (II) ions bridged by a water molecule (salmon and red spheres, respectively).
The crystallographic model (PDB [[6pup]]) contains two Mn (II) ions bridged by a water molecule (salmon and red spheres, respectively).
*<scene name='91/913474/Cv/14'>1st view</scene>.
*<scene name='91/913474/Cv/14'>1st view</scene>.
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*<scene name='91/913474/Cv/15'>2nd view after ~180° rotation</scene>.
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*<scene name='91/913474/Cv/15'>2nd view after ~180° rotation around the vertical axis</scene>.
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<span class="bg-yellow"><span class="far fa-hand-point-right"></span> Remember to drag the structures with the mouse to rotate them.</span>
<scene name='91/913474/Cv/21'>FMN binding site</scene>. FMN is in yellow ball-and-stick representation. The residues contacting FMN, hydrogen bonds (white dashed lines), and selected water molecules (red spheres) are shown. The TYW1 residues are in pink.
<scene name='91/913474/Cv/21'>FMN binding site</scene>. FMN is in yellow ball-and-stick representation. The residues contacting FMN, hydrogen bonds (white dashed lines), and selected water molecules (red spheres) are shown. The TYW1 residues are in pink.
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TYW1 structural similarity to enzymes which couple FAD/FMN and NADP(H) coenzymes for their activity, together with the presence of an unexpected metal binding site, point to a very complex regulation of TYW1 by cell energy metabolism.
TYW1 structural similarity to enzymes which couple FAD/FMN and NADP(H) coenzymes for their activity, together with the presence of an unexpected metal binding site, point to a very complex regulation of TYW1 by cell energy metabolism.
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'''PDB references:''' 1.9 A crystal structure of flavodoxin-like domain of ''Schizosaccharomyces japonicus'' putative tRNAPhe 4-demethylwyosine synthase TYW1 in complex with FMN [[6pup]]; 1.56 A crystal structure of flavodoxin-like domain of ''Schizosaccharomyces japonicus'' putative tRNAPhe 4-demethylwyosine synthase TYW1 in complex with FMN [[6puq]].
<b>References</b><br>
<b>References</b><br>

Current revision

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Alexander Berchansky, Jaime Prilusky

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