3COC: Crystal Structure Of D115a Mutant Of Bacteriorhodopsin

Understanding the energetics of molecular interactions is fundamental to all of the central quests of structural biology including structure prediction and design, mapping evolutionary pathways, learning how mutations cause disease, drug design, and relating structure to function. Hydrogen-bonding is widely regarded as an important force in a membrane environment because of the low dielectric constant of membranes and a lack of competition from water. Indeed, polar residue substitutions are the most common disease-causing mutations in membrane proteins. Because of limited structural information and technical challenges, however, there have been few quantitative tests of hydrogen-bond strength in the context of large membrane proteins. Here we show, by using a double-mutant cycle analysis, that the average contribution of eight interhelical side-chain hydrogen-bonding interactions throughout bacteriorhodopsin is only 0.6 kcal mol(-1). In agreement with these experiments, we find that 4% of polar atoms in the non-polar core regions of membrane proteins have no hydrogen-bond partner and the lengths of buried hydrogen bonds in soluble proteins and membrane protein transmembrane regions are statistically identical. Our results indicate that most hydrogen-bond interactions in membrane proteins are only modestly stabilizing. Weak hydrogen-bonding should be reflected in considerations of membrane protein folding, dynamics, design, evolution and function.
PDB ID: 3COCDownload
MMDB ID: 63747
PDB Deposition Date: 2008/3/27
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2.31  Å
Source Organism:
Similar Structures:
Biological Unit for 3COC: monomeric; determined by author
Molecular Components in 3COC
Label Count Molecule
Protein (1 molecule)
Bacteriorhodopsin(Gene symbol: VNG_RS05715)
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

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