4EDE

Crystal Structure of the Q108K:K40L:T51V:T53C:Y19W:R58W:T29L:A33W Mutant of Cellular Retinol Binding Protein Type II in Complex with All-trans-Retinal at 1.4 Angstrom Resolution

Summary for 4EDE

• Entry DOI: 10.2210/pdb4ede/pdb
• Related: 4EEJ 4EFG
• Descriptor: Retinol-binding protein 2, ACETATE ION, RETINAL, ... (4 entities in total)
• Functional Keywords: retinal complex, beta barrel, transport protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P50120
• Total number of polymer chains: 2
• Total formula weight: 32210.53

Authors

Nossoni, Z.,Geiger, J.H. (deposition date: 2012-03-27, release date: 2012-12-26, 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)