AI Article Synopsis
- Arabidopsis thaliana temperature-induced lipocalin (AtTIL) is a key plant protein involved in stress responses and has a unique ability to bind various molecules, though the exact mechanism is still not fully understood.* -
- The researchers determined the 1.9-Å crystal structure of AtTIL in combination with heme, finding a weak binding interaction with a dissociation constant of about 2 micromolar.* -
- While binding to other potential ligands like retinal and biliverdin was not observed, comparisons with similar proteins suggest it might still occur, marking AtTIL as a structural and functional equivalent of the bacterial lipocalin Blc.*
Article Abstract
Arabidopsis thaliana temperature-induced lipocalin (AtTIL) is a prototypical member of plant lipocalins and participates in a variety of cellular processes, particularly stress responses. Bioinformatical and physiological studies have proposed its promiscuous ligand-binding ability, but the molecular basis is yet unclear. Here, we report the 1.9-Å crystal structure of AtTIL in complex with heme. Spectrophotometric absorbance titration with heme yields a dissociation constant of ∼2 micromolar, indicating the relatively weak interaction between AtTIL and heme, which is confirmed by the AtTIL-heme structure. Although binding to retinal or biliverdin is not detected, such possibility can not be precluded as suggested by comparison with other lipocalin structures. These results show that AtTIL is a structural and functional homolog of the bacterial lipocalin Blc.
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| http://dx.doi.org/10.1016/j.bbagen.2023.130540 | DOI Listing |
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