Anum-II: Difference between revisions
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<StructureSection load="1mg6" size="400" color="" frame="true" spin="on" Scene= | <StructureSection load="1mg6" size="400" color="" frame="true" spin="on" Scene= side="right" caption= > | ||
== '''Introduction''' == | == '''Introduction''' == | ||
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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 <scene name='Sandbox136/Disulfide/1'>disulfide bonds </scene> ([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 <scene name='Sandbox136/Site_catalytique/2'>catalityc apparatus</scene> 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 <scene name='Sandbox136/Disulfide/1'>disulfide bonds </scene> ([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 <scene name='Sandbox136/Site_catalytique/2'>catalityc apparatus</scene> are conserved (<scene name='49/497100/Active_site_residues_with_fas/2'>His48,Tyr52, Tyr73 and Asp99</scene>) 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) 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: | 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: | ||