5EH4: Crystal Structure of the Glycophorin A Transmembrane Dimer in Lipidic Cubic Phase

The mechanisms of assembly and function for many important type I/II (single-pass) transmembrane (TM) receptors are proposed to involve the formation and/or alteration of specific interfaces among their membrane-embedded alpha-helical TM domains. The application of lipidic cubic phase (LCP) bilayer media for crystallization of single-alpha-helical TM complexes has the potential to provide valuable structural and mechanistic insights into many such systems. However, the fidelity of the interfaces observed in crowded crystalline arrays has been difficult to establish from the very limited number of such structures determined using X-ray diffraction data. Here we examine this issue using the glycophorin A (GpA) model system, whose homodimeric TM helix interface has been characterized by solution and solid-state NMR and biochemical techniques but never crystallographically. We report that a GpA-TM peptide readily crystallized in a monoolein cubic phase bilayer, yielding a dimeric alpha-helical structure that is in excellent agreement with previously reported NMR measurements made in several different types of host media. These results provide compelling support for the wider application of LCP techniques to enable X-ray crystallographic analysis of single-pass TM interactions.
PDB ID: 5EH4Download
MMDB ID: 135066
PDB Deposition Date: 2015/10/28
Updated in MMDB: 2015/12
Experimental Method:
x-ray diffraction
Resolution: 2.81  Å
Source Organism:
Similar Structures:
Biological Unit for 5EH4: dimeric; determined by author and by software (PISA)
Molecular Components in 5EH4
Label Count Molecule
Proteins (2 molecules)
Glycophorin-a(Gene symbol: GYPA)
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB