Frataxin: Difference between revisions

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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 edge</scene> around the channel. This hydrophobic entrance may be useful in guiding the Fe 2+ ions into 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).

Within the channel, the metal ion binds at around 4 Å from the side chains of the three Asp 143 residues. 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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Revision as of 22:16, 17 June 2018 view source Rebeca B. Candia (talk \| contribs) 125 edits New page: ==Frataxin== <StructureSection load='2fql' size='340' side='right' caption='Caption for this structure' scene='78/788815/Spacefill_model/1'> == Function and Structural highlights == '''G...		Revision as of 22:42, 17 June 2018 view source Rebeca B. Candia (talk \| contribs) 125 edits No edit summary Newer edit →
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	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 edge</scene> around the channel. This hydrophobic entrance may be useful in guiding the Fe 2+ ions into 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).		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 edge</scene> around the channel. This hydrophobic entrance may be useful in guiding the Fe 2+ ions into 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).

	Within the channel, the metal ion binds at around 4 Å from the side chains of the three Asp 143 residues. 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.