Sandbox Reserved 1069: Difference between revisions

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Yiip's complete protein structure is identified as a dimer. Each [https://en.wikipedia.org/wiki/Monomer monomer] structure is classified into two different domains, the Trans-Membrane Domain (TMD) and C-Terminus Domain (CTD). The TMD consists of six helices, forming binding site A, four of which are oriented in a parallel manner, with respect to each other, while the remaining two are aligned anti parallel to this four helix cluster. A "<scene name='69/694234/Bridge/1'>salt bridge</scene>" or "charge interlock" consisting of four amino acid residues, two [https://en.wikipedia.org/wiki/Lysine Lysines] (Lys 77) and two [https://en.wikipedia.org/wiki/Aspartic_acid Aspartates] (Asp 207), forms a junction that both monomers of Yiip converge at, forming a pivot point for conformation changes. A large portion of the protein containing binding site C, approximately 30 Å in length<sup>[1]</sup>, protrudes into the cytoplasm functioning as a zinc sensor within the cell.

YiiP is a homodimer with each protomer consisting of 238 residues. YiiP has a "Y" shape <scene name='75/756372/Newmainpic/1'> conformation</scene> with two different functional conformations. A total of six helices comprise the transmembrane portion of each <scene name='75/756372/Sixhelices/1'>protomer</scene>. Four of these helices are bundled together while the remaining two are oriented antiparallel to the <scene name='75/756372/2antiparallel/1'>bundle</scene>. Movement of these helices play a role in the function of YiiP. An interlocked salt bridge connects the two domains with the Lys77 and the Asp207 from each protomer - visualized <scene name='75/756372/Saltbridgeclose/1'>here</scene>.This salt bridge acts as the hinge for the conformational changes that YiiP undergoes. YiiP has three zinc binding sites, two of which are known to play an active role in the function of YiiP. Site A (link) sits in extracellular space outside of the cell, while site C is situated inside of the cell to act as a sensor of intracellular zinc concentrations.

YiiP is a homodimer with each protomer consisting of 238 residues. YiiP has a "Y" shape <scene name='75/756372/Newmainpic/1'> conformation</scene> with two different functional conformations. A total of six helices comprise the transmembrane portion of each <scene name='75/756372/Sixhelices/1'>protomer</scene>. Four of these helices are bundled together while the remaining two are oriented antiparallel to the <scene name='75/756372/2antiparallel/1'>bundle</scene>. Movement of these helices play a role in the function of YiiP. An interlocked salt bridge connects the two domains with the Lys77 and the Asp207 from each protomer - visualized <scene name='75/756372/Saltbridgeclose/1'>here</scene>.This [https://en.wikipedia.org/wiki/Salt_bridge_(protein_and_supramolecular) salt bridge] acts as the hinge for the conformational changes that YiiP undergoes. YiiP has three zinc binding sites, two of which are known to play an active role in the function of YiiP. Site A (link) sits in extracellular space outside of the cell, while site C is situated inside of the cell to act as a sensor of intracellular zinc concentrations.

=== Structural highlights ===

Sandbox Reserved 1069: Difference between revisions

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 Yiip's complete protein structure is identified as a dimer. Each [https://en.wikipedia.org/wiki/Monomer monomer] structure is classified into two different domains, the Trans-Membrane Domain (TMD) and C-Terminus Domain (CTD). The TMD consists of six helices, forming binding site A, four of which are oriented in a parallel manner, with respect to each other, while the remaining two are aligned anti parallel to this four helix cluster. A "<scene name='69/694234/Bridge/1'>salt bridge</scene>" or "charge interlock" consisting of four amino acid residues, two [https://en.wikipedia.org/wiki/Lysine Lysines] (Lys 77) and two [https://en.wikipedia.org/wiki/Aspartic_acid Aspartates] (Asp 207), forms a junction that both monomers of Yiip converge at, forming a pivot point for conformation changes. A large portion of the protein containing binding site C, approximately 30 Å in length<sup>[1]</sup>, protrudes into the cytoplasm functioning as a zinc sensor within the cell.
-YiiP is a homodimer with each protomer consisting of 238 residues. YiiP has a "Y" shape <scene name='75/756372/Newmainpic/1'> conformation</scene> with two different functional conformations. A total of six helices comprise the transmembrane portion of each <scene name='75/756372/Sixhelices/1'>protomer</scene>. Four of these helices are bundled together while the remaining two are oriented antiparallel to the <scene name='75/756372/2antiparallel/1'>bundle</scene>. Movement of these helices play a role in the function of YiiP. An interlocked salt bridge connects the two domains with the Lys77 and the Asp207 from each protomer - visualized <scene name='75/756372/Saltbridgeclose/1'>here</scene>.This salt bridge acts as the hinge for the conformational changes that YiiP undergoes. YiiP has three zinc binding sites, two of which are known to play an active role in the function of YiiP. Site A (link) sits in extracellular space outside of the cell, while site C is situated inside of the cell to act as a sensor of intracellular zinc concentrations.
+YiiP is a homodimer with each protomer consisting of 238 residues. YiiP has a "Y" shape <scene name='75/756372/Newmainpic/1'> conformation</scene> with two different functional conformations. A total of six helices comprise the transmembrane portion of each <scene name='75/756372/Sixhelices/1'>protomer</scene>. Four of these helices are bundled together while the remaining two are oriented antiparallel to the <scene name='75/756372/2antiparallel/1'>bundle</scene>. Movement of these helices play a role in the function of YiiP. An interlocked salt bridge connects the two domains with the Lys77 and the Asp207 from each protomer - visualized <scene name='75/756372/Saltbridgeclose/1'>here</scene>.This [https://en.wikipedia.org/wiki/Salt_bridge_(protein_and_supramolecular) salt bridge] acts as the hinge for the conformational changes that YiiP undergoes. YiiP has three zinc binding sites, two of which are known to play an active role in the function of YiiP. Site A (link) sits in extracellular space outside of the cell, while site C is situated inside of the cell to act as a sensor of intracellular zinc concentrations.
 === Structural highlights ===