Garman lab: Interconversion of lysosomal enzyme specificities: Difference between revisions
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<jmol> | <jmol> | ||
<jmolButton> | <jmolButton> | ||
<script>!exit; ppdiaCaptionCmd = "changeCaption('The enyme GAL (green) in complex with the sugar galactose. ','white','black');"; javascript @ppdiaCaptionCmd | <script>!exit; ppdiaCaptionCmd = "changeCaption('The enyme GAL (green) in complex with the sugar galactose. ','white','black');"; javascript @ppdiaCaptionCmd; model 1</script> | ||
<text>GAL</text> | <text>GAL</text> | ||
</jmolButton> | </jmolButton> | ||
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<jmolButton> | <jmolButton> | ||
<script>!exit; ppdiaCaptionCmd = "changeCaption('The enyme NAGAL (blue) in complex with the sugar N-acetyl galactosamin. ','white','black');"; | <script>!exit; ppdiaCaptionCmd = "changeCaption('The enyme NAGAL (blue) in complex with the sugar N-acetyl galactosamin. ','white','black');"; | ||
javascript @ppdiaCaptionCmd | javascript @ppdiaCaptionCmd;model 2</script> | ||
<text>NAGAL</text> | <text>NAGAL</text> | ||
</jmolButton> | </jmolButton> | ||
</jmol> <jmol> | </jmol> <jmol> | ||
<jmolButton> | <jmolButton> | ||
<script>!exit; ppdiaCaptionCmd = "changeCaption('Superposition of GAL (green) and NAGAL (blue).','white','black');"; javascript @ppdiaCaptionCmd | <script>!exit; ppdiaCaptionCmd = "changeCaption('Superposition of GAL (green) and NAGAL (blue).','white','black');"; javascript @ppdiaCaptionCmd; model 0</script> | ||
<text>both</text> | <text>both</text> | ||
</jmolButton> | </jmolButton> | ||
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GAL(SA) is derived from GAL by replacing actives site residues glutamate 203 with serine and leucine 206 with alanine. Having these smaller amino acids in the active site increases the substrate binding cavity, and makes the active site of αGAL(SA) very similar to that of αNAGAL. With these substitutions, the catalytic activity of GAL(SA) is more similar to NAGAL than to GAL (the data is not shown here, but can be found in the research paper<ref name=primary/>). | GAL(SA) is derived from GAL by replacing actives site residues glutamate 203 with serine and leucine 206 with alanine. Having these smaller amino acids in the active site increases the substrate binding cavity, and makes the active site of αGAL(SA) very similar to that of αNAGAL. With these substitutions, the catalytic activity of GAL(SA) is more similar to NAGAL than to GAL (the data is not shown here, but can be found in the research paper<ref name=primary/>). | ||
<jmol><jmolLink><script>script "/scripts/78/786673/Fig2a_galnac_complex/ | <jmol><jmolLink><script>script "/scripts/78/786673/Fig2a_galnac_complex/3.spt"; ppdiaCaptionCmd = "changeCaption('Crystal structure of GAL(SA) bound to N-acetyl galactosamine. GAL(SA) active site residues are shown in yellow and the product, N-acetyl galactosamine, is shown in gray. The blue mesh around the sugar represents its (2Fo-Fc) electron density.','white','black');";javascript @ppdiaCaptionCmd;model 2; model 2</script><text>Panel A</text></jmolLink></jmol>: in complex with N-acetyl galactosamine | ||
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</jmol> | </jmol> | ||
<jmol><jmolLink><script>script "/scripts/78/786673/Galsa_gal/ | <jmol><jmolLink><script>script "/scripts/78/786673/Galsa_gal/2.spt"; ppdiaCaptionCmd = "changeCaption('Crystal structure of GAL(SA) bound to galactose. GAL(SA) active site residues are shown in yellow and the product, galactose, is shown in gray. The blue mesh around the sugar represents its (2Fo-Fc) electron density.','white','black');";javascript @ppdiaCaptionCmd;model 2; model 2</script><text>Panel B</text></jmolLink></jmol>: in complex with galactose | ||
<jmol> | <jmol> | ||