Sandbox Reserved 711: Difference between revisions

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The endopolygalacturonase II from Aspergillus niger has a beta-helix structure<ref>http://www.ncbi.nlm.nih.gov/pubmed/10521427</ref>: the chain folds into 10 turns, shaping the faces of a right-handed helix consisting in 4 parallel beta-sheets - PB1, PB2a, PB2b and PB3 - separated by loops. The helix is closed at its N-terminal end by a small alpha-helix.

4 disulfide bridges, conserved in all endopolygalacturonases of ''A. Niger'', hold together different parts of the chain, and particularily one of these attaches the N-terminal helix to the PB2b sheet.

The loops separating PB1 and PB2a 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.

Sandbox Reserved 711: Difference between revisions

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 The endopolygalacturonase II from Aspergillus niger has a beta-helix structure<ref>http://www.ncbi.nlm.nih.gov/pubmed/10521427</ref>: the chain folds into 10 turns, shaping the faces of a right-handed helix consisting in 4 parallel beta-sheets - PB1, PB2a, PB2b and PB3 - separated by loops. The helix is closed at its N-terminal end by a small alpha-helix.
 disulfide bridges, conserved in all endopolygalacturonases of ''A. Niger'', hold together different parts of the chain, and particularily one of these attaches the N-terminal helix to the PB2b sheet.
-The loops separating PB1 and PB2a 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.
 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.