Sandbox Reserved 711: Difference between revisions
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The <scene name='Sandbox_Reserved_711/Chain_b_cleft/1'>loops separating PB1 and PB2a</scene> are longer on the C-terminal end, and those between PB3 and PB1 on the N-terminal end, what forms a cleft between two extensions outside of the the beta-helix. Its shape, open at both ends of the protein, allows the fixation of a linear glucidic chain, and is suited to the endohydrolytic mode of action. This cleft is a higly conserved region. | The <scene name='Sandbox_Reserved_711/Chain_b_cleft/1'>loops separating PB1 and PB2a</scene> are longer on the C-terminal end, and those between PB3 and PB1 on the N-terminal end, what forms a cleft between two extensions outside of the the beta-helix. Its shape, open at both ends of the protein, allows the fixation of a linear glucidic chain, and is suited to the endohydrolytic mode of action. This cleft is a higly conserved region. | ||
<scene name='Sandbox_Reserved_711/Active_site_residues/1'>8 particular amino-acids</scene> in this region are strictly conserved among polygalacturonases from other fungal and bacterial species: Asn178, Asp180, Asp201, Asp202, His223, Gly224, Arg256, and Lys258. | <scene name='Sandbox_Reserved_711/Active_site_residues/1'>8 particular amino-acids</scene> in this region are strictly conserved among polygalacturonases from other fungal and bacterial species: Asn178, Asp180, Asp201, Asp202, His223, Gly224, Arg256, and Lys258 (shown in red). | ||
The residues directly involved in the catalytic activity seem to be <scene name='Sandbox_Reserved_711/Active_site_residues/3'>Asp180, Asp201, Asp202, and His223</scene>, that form a plane above which space is available, while <scene name='Sandbox_Reserved_711/Active_site_residues/4'>Arg256 and Lys258 </scene> would bind the substrate.<scene name='Sandbox_Reserved_711/Active_site_residues/5'>Gly224</scene>, at the bottom of the cleft, doesn't point out of the helix. | The residues directly involved in the catalytic activity seem to be <scene name='Sandbox_Reserved_711/Active_site_residues/3'>Asp180, Asp201, Asp202, and His223</scene> (orange), that form a plane above which space is available, while <scene name='Sandbox_Reserved_711/Active_site_residues/4'>Arg256 and Lys258 </scene> (light pink) would bind the substrate.<scene name='Sandbox_Reserved_711/Active_site_residues/5'>Gly224</scene> (dark pink), at the bottom of the cleft, doesn't point out of the helix. | ||
== Endo-polygalacturonase II applications == | == Endo-polygalacturonase II applications == | ||