9UPN

Cryo-EM structure of macaque green cone pigment with Q114N mutation

Summary for 9UPN

• Entry DOI: 10.2210/pdb9upn/pdb
• EMDB information: 64398
• Descriptor: MW opsin,Soluble cytochrome b562, RETINAL (2 entities in total)
• Functional Keywords: visual pigment, gpcr, rhodopsin, membrane protein
• Biological source: Macaca fascicularis (crab-eating macaque); More
• Total number of polymer chains: 1
• Total formula weight: 48612.29

Authors

Ohashi, S.,Kojima, A.,Fukuda, M.,Kim, S.,Kato, H.E.,Kandori, H.,Katayama, K. (deposition date: 2025-04-28, release date: 2026-06-24, Last modification date: 2026-07-08)

Primary citation

Ohashi, S.,Katayama, K.,Kojima, A.,Yang, X.,Fukuda, M.,Sacchetta, F.,Suno, R.,Sugita, Y.,Nuemket, N.,Kim, S.,Kobayashi, K.,Imai, H.,Iwata, S.,Nango, E.,Kobayashi, T.,Noda, T.,Olivucci, M.,Kato, H.E.,Kandori, H.
Structural insights into spectral tuning and retinal exchange in cone visual pigments.
Science, 392:eadz3996-eadz3996, 2026

PubMed Abstract: Color vision in catarrhine primates relies on red-, green-, and blue-sensitive cone pigments that share an 11--retinal chromophore but differ in absorption maxima. Red and green pigments arose by recent gene duplication and differ at only a few residues. Here, we report cryo-electron microscopy structures of red and green cone pigments from the cynomolgus macaque () integrated with low-temperature vibrational spectroscopy and quantum mechanical and molecular mechanical modeling. The red-green spectral shift is dominated by threonine 285, the hydroxyl dipole of which modulates chromophore electrostatics, whereas steric effects appear modest. We also identified membrane-facing lateral openings in cone pigments but not in inactive rhodopsin. Comparisons with active-state structures suggest activation-dependent gating, and mutational and spectroscopic analyses support a role for this opening in retinal uptake and rapid pigment regeneration.

PubMed: 42348681
DOI: 10.1126/science.adz3996

Experimental method

ELECTRON MICROSCOPY (3.37 Å)