7BZG
Structure of Bacillus subtilis HxlR, wild type in complex with formaldehyde and DNA
Summary for 7BZG
| Entry DOI | 10.2210/pdb7bzg/pdb |
| Related | 7BZD |
| Descriptor | HTH-type transcriptional activator HxlR, DNA (5'-D(*CP*AP*GP*TP*AP*TP*CP*CP*TP*CP*GP*AP*GP*GP*AP*TP*AP*CP*TP*G)-3'), FORMYL GROUP, ... (8 entities in total) |
| Functional Keywords | transcriptional regulator, formaldehyde sensing, dna binding protein, dna binding protein-dna complex |
| Biological source | Bacillus subtilis (strain 168) More |
| Total number of polymer chains | 12 |
| Total formula weight | 124817.08 |
| Authors | Zhu, R.,Chen, P.R. (deposition date: 2020-04-27, release date: 2021-02-03, Last modification date: 2024-11-20) |
| Primary citation | Zhu, R.,Zhang, G.,Jing, M.,Han, Y.,Li, J.,Zhao, J.,Li, Y.,Chen, P.R. Genetically encoded formaldehyde sensors inspired by a protein intra-helical crosslinking reaction. Nat Commun, 12:581-581, 2021 Cited by PubMed Abstract: Formaldehyde (FA) has long been considered as a toxin and carcinogen due to its damaging effects to biological macromolecules, but its beneficial roles have been increasingly appreciated lately. Real-time monitoring of this reactive molecule in living systems is highly desired in order to decipher its physiological and/or pathological functions, but a genetically encoded FA sensor is currently lacking. We herein adopt a structure-based study of the underlying mechanism of the FA-responsive transcription factor HxlR from Bacillus subtilis, which shows that HxlR recognizes FA through an intra-helical cysteine-lysine crosslinking reaction at its N-terminal helix α1, leading to conformational change and transcriptional activation. By leveraging this FA-induced intra-helical crosslinking and gain-of-function reorganization, we develop the genetically encoded, reaction-based FA sensor-FAsor, allowing spatial-temporal visualization of FA in mammalian cells and mouse brain tissues. PubMed: 33495458DOI: 10.1038/s41467-020-20754-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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