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. | ||
8 particular amino-acids 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. | ||
The residues directly involved in the catalytic activity seem to be Asp180, Asp201, Asp202, and His223, that form a plane above which space is available, while Arg256 and Lys258 would bind the substrate. Gly224, at the bottom of the cleft, doesn't point out of the helix. | The residues directly involved in the catalytic activity seem to be Asp180, Asp201, Asp202, and His223, that form a plane above which space is available, while Arg256 and Lys258 would bind the substrate. Gly224, at the bottom of the cleft, doesn't point out of the helix. | ||