Structural Basis for Autoregulation of the Zinc Transporter YiiP

Journal Article · Thu Jan 01 00:00:00 EST 2009 · Nature Structural and Molecular Biology

DOI:https://doi.org/10.1038/nsmb.1662· OSTI ID:980501

Lu, M; Chai, J; Fu, D

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.

• Research Organization: Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: DE-AC02-98CH10886
• OSTI ID: 980501
• Report Number(s): BNL-93419-2010-JA; TRN: US201015%%1886
• Journal Information: Nature Structural and Molecular Biology, Vol. 16; ISSN 1072-8368
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
CHEMISTRY
CONTROL
DIMERS
ENERGY TRANSFER
ESCHERICHIA COLI
FLUCTUATIONS
FLUORESCENCE
GEOMETRY
INTERFACES
INTERLOCKS
METALS
PROGRAMMING LANGUAGES
PROTEINS
RESOLUTION
RESONANCE
SALTS
TRANSPORT
ZINC
national synchrotron light source