6HMJ

Structure of an RNA-binding Light-Oxygen-Voltage Receptor

Summary for 6HMJ

• Entry DOI: 10.2210/pdb6hmj/pdb
• Descriptor: Putative PAS/PAC sensor protein, FLAVIN MONONUCLEOTIDE, GLYCEROL, ... (6 entities in total)
• Functional Keywords: sensory photoreceptor, light-oxygen-voltage, rna binding, signaling protein
• Biological source: Nakamurella multipartita DSM 44233 (Microsphaera multipartita)
• Total number of polymer chains: 4
• Total formula weight: 163981.49

Authors

Ziegler, T.,Moniot, S.,Moeglich, A. (deposition date: 2018-09-12, release date: 2019-08-28, Last modification date: 2024-05-15)

Primary citation

Weber, A.M.,Kaiser, J.,Ziegler, T.,Pilsl, S.,Renzl, C.,Sixt, L.,Pietruschka, G.,Moniot, S.,Kakoti, A.,Juraschitz, M.,Schrottke, S.,Lledo Bryant, L.,Steegborn, C.,Bittl, R.,Mayer, G.,Moglich, A.
A blue light receptor that mediates RNA binding and translational regulation.
Nat.Chem.Biol., 15:1085-1092, 2019

PubMed Abstract: Sensory photoreceptor proteins underpin light-dependent adaptations in nature and enable the optogenetic control of organismal behavior and physiology. We identified the bacterial light-oxygen-voltage (LOV) photoreceptor PAL that sequence-specifically binds short RNA stem loops with around 20 nM affinity in blue light and weaker than 1 µM in darkness. A crystal structure rationalizes the unusual receptor architecture of PAL with C-terminal LOV photosensor and N-terminal effector units. The light-activated PAL-RNA interaction can be harnessed to regulate gene expression at the RNA level as a function of light in both bacteria and mammalian cells. The present results elucidate a new signal-transduction paradigm in LOV receptors and conjoin RNA biology with optogenetic regulation, thereby paving the way toward hitherto inaccessible optoribogenetic modalities.

PubMed: 31451761
DOI: 10.1038/s41589-019-0346-y

Experimental method

X-RAY DIFFRACTION (2.51 Å)