Membrane biophysics articles within Nature

Featured

• Letter | 21 October 2012

  Structure and mechanism of a bacterial sodium-dependent dicarboxylate transporter

  The cytosolic concentration of citrate partially depends on its direct import across the plasma membrane by the Na⁺-dependent citrate transporter (NaCT); here the X-ray crystal structure of a bacterial homologue of NaCT is reported, which, along with transport-activity studies, suggests how specific conformational changes facilitate substrate translocation across the cellular membrane.

  • Romina Mancusso
  • , G. Glenn Gregorio
  •  & Da-Neng Wang

• Letter | 02 September 2012

  Alternating-access mechanism in conformationally asymmetric trimers of the betaine transporter BetP

  The crystal structure of the osmotically regulated symporter BetP is reported in four new conformations, providing information about the key conformational changes that take place during the transport cycle.

  • Camilo Perez
  • , Caroline Koshy
  •  & Christine Ziegler

• Letter | 18 December 2011

  Subnanometre-resolution structure of the intact Thermus thermophilus H⁺-driven ATP synthase

  Insights into the rotary mechanism of the Thermus thermophilus ATP synthase are obtained using electron cryomicroscopy to determine its three-dimensional structure calculated to subnanometre resolution.

  • Wilson C. Y. Lau
  •  & John L. Rubinstein

• Letter | 23 October 2011

  Aspartate 112 is the selectivity filter of the human voltage-gated proton channel

  • Boris Musset
  • , Susan M. E. Smith
  •  & Thomas E. DeCoursey

• Letter | 09 September 2010

  Structural basis of Na⁺-independent and cooperative substrate/product antiport in CaiT

  Transport of solutes across biological membranes is carried out by specialized secondary transport proteins in the lipid bilayer. These authors report structures of the sodium-independent carnitine/butyrobetaine antiporter CaiT from two microorganisms. The three-dimensional architecture of CaiT resembles that of the Na⁺-dependent transporters LeuT and BetP, but in CaiT a methionine sulphur takes the place of the Na⁺ ion to coordinate the substrate in the central transport site, enabling Na⁺-independent transport to occur.

  • Sabrina Schulze
  • , Stefan Köster
  •  & Werner Kühlbrandt

• News & Views | 27 January 2010

  Joint effort bends membrane

  The curvature of cellular membranes is generated by proteins and lipids. A synthetic experimental system allows the interplay between protein- and lipid-generated bending mechanisms to be studied directly.

  • Michael M. Kozlov