8il9

Crystal structure of the LOV1 Q122N mutant of Klebsormidium nitens phototropin

spinqualitylabelsall models 8il9, resolution 2.16Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8il9 is a 1 chain structure with sequence from Klebsormidium nitens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.16Å Ligands: FMN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1Y1HNG4_KLENI Publication Abstract from PubMed 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 (tau = 41 +/- 3 min) compared to different mutants (R60K: tau = 2.0 +/- 0.1 min, Q122N: tau = 1.7 +/- 0.1 min, D33N: tau = 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. Unusual photodynamic characteristics of the light-oxygen-voltage domain of phototropin linked to terrestrial adaptation of Klebsormidium nitens.,Sharma S, Gautam AK, Singh R, Gourinath S, Kateriya S FEBS J. 2024 Sep 29. doi: 10.1111/febs.17284. PMID:39344087 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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