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is an integral membrane protein of the E. coli bacteria that regulates the import and export of Zn²⁺. This regulation prevents zinc toxicity and deprivation within the cytoplasm, which can lead to cell death.

Structure

Yiip's complete protein structure is identified as a dimer. Each 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 "" or "charge interlock" consisting of four amino acid residues, two Lysines (Lys 77) and two 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^[1], protrudes into the cytoplasm functioning as a zinc sensor within the cell.

Salt Bridge

Electrostatic Interactions

Electrostatic Charge Distribution

Conformation Changes