8I11

Crystal structure of LOV1 domain of phototropin from Klebsormidium nitens

Summary for 8I11

• Entry DOI: 10.2210/pdb8i11/pdb
• Descriptor: Phototropin, FLAVIN MONONUCLEOTIDE (3 entities in total)
• Functional Keywords: electron transport, flavoprotein
• Biological source: Klebsormidium nitens
• Total number of polymer chains: 1
• Total formula weight: 17466.66

Authors

Gautam, A.K.,Sharma, S.,Gourinath, S.,Kateriya, S. (deposition date: 2023-01-12, release date: 2024-01-24, Last modification date: 2024-12-18)

Primary citation

Sharma, S.,Gautam, A.K.,Singh, R.,Gourinath, S.,Kateriya, S.
Unusual photodynamic characteristics of the light-oxygen-voltage domain of phototropin linked to terrestrial adaptation of Klebsormidium nitens.
Febs J., 291:5156-5176, 2024

PubMed Abstract: Phototropin (Phot), a blue light-sensing LOV domain protein, mediates blue light responses and is evolutionarily conserved across the green lineage. Klebsormidium nitens, a green terrestrial alga, presents a valuable opportunity to study adaptive responses from aquatic to land habitat transitions. We determined the crystal structure of Klebsormidium nitens Phot LOV1 domain (KnLOV1) in the dark and engineered different mutations (R60K, Q122N, and D33N) to modulate the lifetime of the photorecovery cycle. We observed unusual, slow recovery kinetics in the wild-type KnLOV1 domain (τ = 41 ± 3 min) compared to different mutants (R60K: τ = 2.0 ± 0.1 min, Q122N: τ = 1.7 ± 0.1 min, D33N: τ = 9.6 ± 0.1 min). Crystal structures of wild-type KnLOV1 and mutants revealed subtle but critical changes near the protein chromophore that is responsible for modulating protein dark recovery time. Our findings shed light on the unique structural and biochemical characteristics of the newly studied KnLOV1 and its evolutionary importance for phototropin-mediated physiology.

PubMed: 39344087
DOI: 10.1111/febs.17284

Experimental method

X-RAY DIFFRACTION (1.855 Å)