Sandbox136: Difference between revisions
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Anum-II has a length of 134 amino-acids. The phospholipase is formed by a short N-terminalαhelix (between residues 2-12), a 2nd αhelix (residues 40-55), two-stranded antiparallel <scene name='Sandbox136/Feuillets/1'>sheet</scene> linked thanks to a βwing (74-85) and a 3rd αhelix (residues 90-107). The 3rd αhelix is bound to the 2nd αhelix (in an antiparallele way) thanks to disulfure bonds ([Cys 44-Cys 105] and [Cys 51-Cys 98]) and thus form a <scene name='Sandbox136/Stabilisation/1'>rigid platform</scene>. The protein is stabilized by 5 other disulfides bonds [Cys 27-Cys 125], [Cys 29-Cys 45] [Cys 50 Cys 134] [Cys 61-Cys 91] [Cys84-Cys96]. Alignment of Anum-II with other PLA2 have revealed that the positions of amino-acid residues which form the catalytic apparatus are conserved (His48,Tyr52, Tyr73 and Asp99) except for Asp49 which is replaced by Lys 49. | Anum-II has a length of 134 amino-acids. The phospholipase is formed by a short N-terminalαhelix (between residues 2-12), a 2nd αhelix (residues 40-55), two-stranded antiparallel <scene name='Sandbox136/Feuillets/1'>sheet</scene> linked thanks to a βwing (74-85) and a 3rd αhelix (residues 90-107). The 3rd αhelix is bound to the 2nd αhelix (in an antiparallele way) thanks to disulfure bonds ([Cys 44-Cys 105] and [Cys 51-Cys 98]) and thus form a <scene name='Sandbox136/Stabilisation/1'>rigid platform</scene>. The protein is stabilized by 5 other disulfides bonds [Cys 27-Cys 125], [Cys 29-Cys 45] [Cys 50 Cys 134] [Cys 61-Cys 91] [Cys84-Cys96]. Alignment of Anum-II with other PLA2 have revealed that the positions of amino-acid residues which form the catalytic apparatus are conserved (His48,Tyr52, Tyr73 and Asp99) except for Asp49 which is replaced by Lys 49. | ||
The structure of the protein has revealed the presence of an anion-binding site (Murakami ''et al.'', 2006 | The structure of the protein has revealed the presence of an anion-binding site (Murakami ''et al.'', 2006) between <scene name='Sandbox136/Anion/2'>R34</scene>, <scene name='Sandbox136/Anion/2'>K53</scene> and a water molecule (see Figure 3). Sulfate ion is anchored thanks to hydrogen bonds between: | ||
+O1 atom with R34 Nε , K53 Nζ and a solvent water molecule. | +O1 atom with R34 Nε , K53 Nζ and a solvent water molecule. | ||
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== Bibliography == | == Bibliography == | ||
Holland, D.R., Clancy, L.L., Muchmore, S.W., Ryde, T.J., Einspahr, H.M., Finzel, B.C., Heinrikson, R.L., Watenpaugh, K.D. (1990).''Biochem-J'' .'''265''',17649-56 | |||
Chioato, L., De Oliveira, A. H., Ruller, R., Sa., J. M., Ward, R. J. (2002).''Biochem-J'' .'''366''',971-6 | Chioato, L., De Oliveira, A. H., Ruller, R., Sa., J. M., Ward, R. J. (2002).''Biochem-J'' .'''366''',971-6 | ||
Murakami, M. T. , Melo,C. C., Angulo,Y. , Lomonte,B. Arni, R. K. (2006).''Acta Cryst''.F'''62''', 423-426 | |||
Murakami, M. T. , Melo,C. C., Angulo,Y. , Lomonte,B. Arni, R. K. (2006).''Acta Cryst''.F'''62''', 423-426 | |||
Yamazaki, Y., Matsunaga, Y., Nakano, Y. & Morita, T. (2005). ''J. Biol. Chem''. '''280''', 29989–29992. | Yamazaki, Y., Matsunaga, Y., Nakano, Y. & Morita, T. (2005). ''J. Biol. Chem''. '''280''', 29989–29992. | ||
