3HAO

Crystal structure of bacteriorhodopsin mutant L94A crystallized from bicelles

Summary for 3HAO

• Entry DOI: 10.2210/pdb3hao/pdb
• Related: 3HAN 3HAP 3HAQ 3HAR 3HAS
• Descriptor: Bacteriorhodopsin, RETINAL (3 entities in total)
• Functional Keywords: bacteriorhodopsin, packing force, van der waals, evolutionary constraint, membrane protein, integral membrane protein, helical membrane protein, proton transport, cell membrane, chromophore, hydrogen ion transport, ion transport, membrane, photoreceptor protein, pyrrolidone carboxylic acid, receptor, retinal protein, sensory transduction, transmembrane, transport, transport protein
• Biological source: Halobacterium salinarum (Halobacterium halobium)
• Cellular location: Cell membrane; Multi-pass membrane protein: P02945
• Total number of polymer chains: 2
• Total formula weight: 54343.71

Authors

Joh, N.H.,Yang, D.,Bowie, J.U. (deposition date: 2009-05-02, release date: 2009-09-22, Last modification date: 2024-10-30)

Primary citation

Joh, N.H.,Oberai, A.,Yang, D.,Whitelegge, J.P.,Bowie, J.U.
Similar energetic contributions of packing in the core of membrane and water-soluble proteins.
J.Am.Chem.Soc., 131:10846-10847, 2009

PubMed Abstract: A major driving force for water-soluble protein folding is the hydrophobic effect, but membrane proteins cannot make use of this stabilizing contribution in the apolar core of the bilayer. It has been proposed that membrane proteins compensate by packing more efficiently. We therefore investigated packing contributions experimentally by observing the energetic and structural consequences of cavity creating mutations in the core of a membrane protein. We observed little difference in the packing energetics of water and membrane soluble proteins. Our results imply that other mechanisms are employed to stabilize the structure of membrane proteins.

PubMed: 19603754
DOI: 10.1021/ja904711k

Experimental method

X-RAY DIFFRACTION (2.49 Å)