3H90

Structural basis for the autoregulation of the zinc transporter YiiP

Summary for 3H90

• Entry DOI: 10.2210/pdb3h90/pdb
• Descriptor: Ferrous-iron efflux pump fieF, MERCURY (II) ION, ZINC ION, ... (4 entities in total)
• Functional Keywords: membrane protein, zinc transporter, cell inner membrane, cell membrane, ion transport, iron, iron transport, membrane, transmembrane, transport, transport protein
• Biological source: Escherichia coli K-12
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P69380
• Total number of polymer chains: 4
• Total formula weight: 126546.80

Authors

Lu, M. (deposition date: 2009-04-29, release date: 2009-09-08, Last modification date: 2024-02-21)

Primary citation

Lu, M.,Chai, J.,Fu, D.
Structural basis for autoregulation of the zinc transporter YiiP.
Nat.Struct.Mol.Biol., 16:1063-1067, 2009

PubMed Abstract: Zinc transporters have crucial roles in cellular zinc homeostatic control. The 2.9-A resolution structure of the zinc transporter YiiP from Escherichia coli reveals a richly charged dimer interface stabilized by zinc binding. Site-directed fluorescence resonance energy transfer (FRET) measurements and mutation-activity analysis suggest that zinc binding triggers hinge movements of two electrically repulsive cytoplasmic domains pivoting around four salt bridges situated at the juncture of the cytoplasmic and transmembrane domains. These highly conserved salt bridges interlock transmembrane helices at the dimer interface, where they are well positioned to transmit zinc-induced interdomain movements to reorient transmembrane helices, thereby modulating coordination geometry of the active site for zinc transport. The cytoplasmic domain of YiiP is a structural mimic of metal-trafficking proteins and the metal-binding domains of metal-transporting P-type ATPases. The use of this common structural module to regulate metal coordination chemistry may enable a tunable transport activity in response to cytoplasmic metal fluctuations.

PubMed: 19749753
DOI: 10.1038/nsmb.1662

Experimental method

X-RAY DIFFRACTION (2.9 Å)