Frataxin: Difference between revisions
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The channel of the trimer is formed at its 3-fold axis, in a central position. It is the strure responsible for stabilizing the atom of iron for delivery, but also acts to further stabilise the trimeric form. | The channel of the trimer is formed at its 3-fold axis, in a central position. It is the strure responsible for stabilizing the atom of iron for delivery, but also acts to further stabilise the trimeric form. | ||
Stabilising the | Stabilising one side of the channel, there are some interactions between the <scene name='78/786054/151-155_144-149/1'>loops around the central channel</scene>, which form a helic structure maintened, for instance, through hydrogen bonds between the pairs <scene name='78/786054/152-147_hydrogen_bond/1'>Leu 152-Gly 147</scene> and <scene name='78/786054/146-154_hydrogen_bond/1'>Asn 146-Gln 154</scene>. | ||
In the structure of the channel, the side chains of the hydrophobic aminoacids Leu 145, Val 150 and Leu 152 are exposed to the solvent, creating a <scene name='78/786054/Hydrophobic_lid/3'>hydrophobic | In the structure of the channel, the side chains of the hydrophobic aminoacids Leu 145, Val 150 and Leu 152 are exposed to the solvent, creating a <scene name='78/786054/Hydrophobic_lid/3'>hydrophobic lid</scene> around the channel. This hydrophobic lid isolates one of the sides of the channel core, as well as providing a hydrophobic contact surface by which other proteins can interact, hiding their hydrophobic residues from the solvent-rich environment. | ||
The hydrophobic lid formed by Leu 145, Val 150 and Leu 152 fully encloses the iron atom within the channel (iron atom not shown). | |||
<scene name='78/786054/143-129__hydrogen_bond/1'>Asp 143-Gln 129</scene>,. | |||
Within the channel, the metal ion binds at around 4 Å from the side chains of the <scene name='78/788815/Iron_channel/1'>three Asp 143 residues</scene> (distances between residues are shown for reference). Laboraroty data from X-ray cristallography suggests the Fe 2+ ion being associated with solvent molecules. | Within the channel, the metal ion binds at around 4 Å from the side chains of the <scene name='78/788815/Iron_channel/1'>three Asp 143 residues</scene> (distances between residues are shown for reference). Laboraroty data from X-ray cristallography suggests the Fe 2+ ion being associated with solvent molecules. | ||
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<scene name='78/786054/125-128/2'>125-128</scene> | <scene name='78/786054/125-128/2'>125-128</scene> | ||
<scene name='78/786054/125-128_143_solvent_acess/1'>Solvent acess</scene> | <scene name='78/786054/125-128_143_solvent_acess/1'>Solvent acess</scene> | ||
<scene name='78/786054/Esquema_geral/1'>esquema geral</scene> | <scene name='78/786054/Esquema_geral/1'>esquema geral</scene> | ||
<scene name='78/786054/143-129__hydrogen_bond/1'>143-129 hydrogen bond</scene> | <scene name='78/786054/143-129__hydrogen_bond/1'>143-129 hydrogen bond</scene> | ||
