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

Summary for 4RUU

• Entry DOI: 10.2210/pdb4ruu/pdb
• Related: 4EDE 4EEJ 4EFG 4EXZ 4GKC
• Descriptor: Retinol-binding protein 2, RETINAL, ACETATE ION, ... (4 entities in total)
• Functional Keywords: wavelength regulation, transport protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P50120
• Total number of polymer chains: 2
• Total formula weight: 31851.92

Authors

Nosrati, M.,Geiger, J.H. (deposition date: 2014-11-21, release date: 2014-12-10, Last modification date: 2024-11-06)

Primary citation

Wang, W.,Nossoni, Z.,Berbasova, T.,Watson, C.T.,Yapici, I.,Lee, K.S.,Vasileiou, C.,Geiger, J.H.,Borhan, B.
Tuning the electronic absorption of protein-embedded all-trans-retinal.
Science, 338:1340-1343, 2012

PubMed Abstract: 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.

PubMed: 23224553
DOI: 10.1126/science.1226135

Experimental method

X-RAY DIFFRACTION (1.4 Å)