4RUU: Crystal structure of the Q108K:K40L mutant of human Cellular Retinol Binding ProteinII in complex with All-trans-Retinal after 24 hour incubation at 1.4 Angstrom Resolution

Protein-chromophore interactions are a central component of a wide variety of critical biological processes such as color vision and photosynthesis. To understand the fundamental elements that contribute to spectral tuning of a chromophore inside the protein cavity, we redesigned human cellular retinol binding protein II (hCRBPII) to fully encapsulate all-trans-retinal and form a covalent bond as a protonated Schiff base. This system, using rational mutagenesis designed to alter the electrostatic environment within the binding pocket of the host protein, enabled regulation of the absorption maximum of the pigment in the range of 425 to 644 nanometers. With only nine point mutations, the hCRBPII mutants induced a systematic shift in the absorption profile of all-trans-retinal of more than 200 nanometers across the visible spectrum.
PDB ID: 4RUUDownload
MMDB ID: 125467
PDB Deposition Date: 2014/11/21
Updated in MMDB: 2017/12
Experimental Method:
x-ray diffraction
Resolution: 1.4  Å
Source Organism:
Similar Structures:
Biological Unit for 4RUU: monomeric; determined by author and by software (PISA)
Molecular Components in 4RUU
Label Count Molecule
Protein (1 molecule)
Retinol-binding Protein 2(Gene symbol: RBP2)
Molecule annotation
Chemicals (2 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB