Sandboxjg: Difference between revisions
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<Structure load='1rd8' size='500' frame='true' align='right' caption='ClC Transporter' scene='Insert optional scene name here' /> | <Structure load='1rd8' size='500' frame='true' align='right' caption='ClC Transporter' scene='Insert optional scene name here' /> | ||
<scene name='Sandboxjg/1ots/2'>CLC-ec1 (1OTS) protein</scene> is a membrane protein Escherichia coli which belongs to the CLC family of ion channels and transporters. These proteins are essential for the maintenance of proper membrane potential in muscle cells, for the transport of electrolytes across epithelial layers, and to. | <scene name='Sandboxjg/1ots/2'>CLC-ec1 (1OTS) protein</scene> is a membrane protein Escherichia coli which belongs to the CLC family of ion channels and transporters. These proteins are essential for the maintenance of proper membrane potential in muscle cells, for the transport of electrolytes across epithelial layers, and to. | ||
Roderick MacKinnon and his team determined the structure of this protein and proposed that it was a Cl- selective ion channel. Accardi and Miller showed that CLC-ec1 functions as a transporter: it exchanges 2 Cl- :1 H+. | Roderick MacKinnon and his team determined the structure of this protein and proposed that it was a Cl- selective ion channel. Accardi and Miller showed that CLC-ec1 functions as a transporter: it exchanges 2 Cl- :1 H+. [[Image:ClCvideoProteopedia.mov]]. | ||
The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane The Cl- and H+ pathways are formed by an extensive network of interactions between the protein and substrates. The Cl- ions are stabilized in the middle of the membrane by the dipole moment of two a-helices, by interactions with amides from the protein’s backbone and by the direct coordination of two conserved side chains. Because each polypeptide chain functions independently, we will focus on the structure of one pore. | The CLC-ec1 transporter is a dimer formed of two polypeptide chains each containing an internal repeat arranged in an anti-parallel organization. Each monomer functions independently of the other and creates a passage for ions through the membrane The Cl- and H+ pathways are formed by an extensive network of interactions between the protein and substrates. The Cl- ions are stabilized in the middle of the membrane by the dipole moment of two a-helices, by interactions with amides from the protein’s backbone and by the direct coordination of two conserved side chains. Because each polypeptide chain functions independently, we will focus on the structure of one pore. | ||
