Sandbox Reserved 828: Difference between revisions

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The tail is structurally conserved although large surface loops emanating from different points give it a different outward appearance It forms a heart-shaped homodimer with two protein interfaces, the DNA- and C-gates. GyrA59 is the minimal fragment of the A-subunit which, when complexed with the B-subunit, has DNA-cleavage activity.

The remaining 30–35 kDa comprising the C-terminal domain (CTD) of GyrA shows a domain forming a b-pinwheel with a positively charged amino-acid perimeter. This carboxy-terminal domain of GyrA (cyan) is required for the introduction of DNA supercoils).

The remaining 30–35 kDa comprising the C-terminal domain (CTD) of GyrA shows a domain forming a b-pinwheel with a positively charged amino-acid perimeter. This carboxy-terminal domain of GyrA (cyan) is required for the introduction of DNA supercoils), DNA wrps around it. It is lnked to the central part of GyraseA by a flexible 13-15 residues region and stands close to the C-gate and may present an up and down movement in the early stades of the catalytic cycle and may be involved in the helping of G segment and D-gate binding so as the CTD binding of DNA.

'''The B protein''' has the ATPase domain and the Toprim fold on it. Two ATPase domains dimerize to form a closed conformation. The Toprim fold is a Rossmann fold (beta-alpha-beta-alpha-beta) that contains three invariant acidic residues that coordinate magnesium ions involved in DNA cleavage and DNA religation.

Sandbox Reserved 828: Difference between revisions

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@@ Line 35: / Line 35: @@
 The tail is structurally conserved  although large surface loops emanating from different points give it a different outward appearance It forms a heart-shaped homodimer with two protein interfaces, the DNA- and C-gates. GyrA59 is the minimal fragment of the A-subunit which, when complexed with the B-subunit, has DNA-cleavage activity.
-The remaining 30–35 kDa comprising the C-terminal domain (CTD) of GyrA shows a domain forming a b-pinwheel with a positively charged amino-acid perimeter. This carboxy-terminal domain of GyrA (cyan) is required for the introduction of DNA supercoils).
+The remaining 30–35 kDa comprising the C-terminal domain (CTD) of GyrA shows a domain forming a b-pinwheel with a positively charged amino-acid perimeter. This carboxy-terminal domain of GyrA (cyan) is required for the introduction of DNA supercoils), DNA wrps around it. It is lnked to the central part of GyraseA by a flexible 13-15 residues region and stands close to the C-gate and may present an up and down movement in the early stades of the catalytic cycle and may be involved in the helping of G segment and D-gate binding so as the CTD binding of DNA.
 '''The B protein''' has the ATPase domain and the Toprim fold on it. Two ATPase domains dimerize to form a closed conformation. The Toprim fold is a Rossmann fold (beta-alpha-beta-alpha-beta) that contains three invariant acidic residues that coordinate magnesium ions involved in DNA cleavage and DNA religation.