Aquaporin Z (AqpZ) (AqpZ)

Aquaporin Z (AqpZ) is a highly selective water channel protein located in the inner membrane of Escherichia coli [1]. As a member of the Major Intrinsic Protein (MIP) family, it forms homotetramers that facilitate the rapid movement of water across the cell membrane in response to osmotic gradients [2]. AqpZ is distinguished by its high selectivity, allowing water molecules to pass while strictly excluding protons and other solutes, a feature essential for maintaining cellular electrochemical gradients [3]. The protein is most active during the exponential growth phase, playing a vital role in the bacteria's ability to adapt to changes in environmental osmolarity [1].\n\nAlthough not currently a target for FDA-approved drugs, AqpZ is inhibited by silver and gold ions and is a significant subject of research for novel antimicrobial development [4]. Its structural homology to human aquaporins makes it an important model for studying the biophysics of water transport and for the design of biomimetic filtration systems [2][3]. Understanding AqpZ function is crucial for insights into bacterial physiology and the development of strategies to disrupt bacterial environmental resilience [1][4]. References: [1] UniProt P0A6Q3; [2] Borgnia et al. (1999) J Mol Biol; [3] Savage et al. (2003) PLoS Biol; [4] Niemietz & Tyerman (2002) J Exp Bot.

Other names

Water channel protein ZaqpZb0875JW0859

Aquaporin Z facilitates the rapid, passive transport of water molecules across the cytoplasmic membrane along an osmotic gradient by providing a low-resistance pathway that excludes protons and other solutes [1][2][3].