7XN2
Crystal structure of CvkR, a novel MerR-type transcriptional regulator
Summary for 7XN2
| Entry DOI | 10.2210/pdb7xn2/pdb | 
| Descriptor | Alr3614 protein, ADENOSINE-5'-TRIPHOSPHATE, DI(HYDROXYETHYL)ETHER, ... (4 entities in total) | 
| Functional Keywords | merr-type transcriptional regulator, transcription | 
| Biological source | Nostoc sp. PCC 7120 = FACHB-418 | 
| Total number of polymer chains | 1 | 
| Total formula weight | 18361.56 | 
| Authors | Liang, Y.J.,Zhu, T.,Ma, H.L.,Lu, X.F.,Hess, W.R. (deposition date: 2022-04-27, release date: 2023-03-08, Last modification date: 2024-05-29)  | 
| Primary citation | Ziemann, M.,Reimann, V.,Liang, Y.,Shi, Y.,Ma, H.,Xie, Y.,Li, H.,Zhu, T.,Lu, X.,Hess, W.R. CvkR is a MerR-type transcriptional repressor of class 2 type V-K CRISPR-associated transposase systems. Nat Commun, 14:924-924, 2023 Cited by  PubMed Abstract: Certain CRISPR-Cas elements integrate into Tn7-like transposons, forming CRISPR-associated transposon (CAST) systems. How the activity of these systems is controlled in situ has remained largely unknown. Here we characterize the MerR-type transcriptional regulator Alr3614 that is encoded by one of the CAST (AnCAST) system genes in the genome of cyanobacterium Anabaena sp. PCC 7120. We identify a number of Alr3614 homologs across cyanobacteria and suggest naming these regulators CvkR for Cas V-K repressors. Alr3614/CvkR is translated from leaderless mRNA and represses the AnCAST core modules cas12k and tnsB directly, and indirectly the abundance of the tracr-CRISPR RNA. We identify a widely conserved CvkR binding motif 5'-AnnACATnATGTnnT-3'. Crystal structure of CvkR at 1.6 Å resolution reveals that it comprises distinct dimerization and potential effector-binding domains and that it assembles into a homodimer, representing a discrete structural subfamily of MerR regulators. CvkR repressors are at the core of a widely conserved regulatory mechanism that controls type V-K CAST systems. PubMed: 36801863DOI: 10.1038/s41467-023-36542-9 PDB entries with the same primary citation  | 
| Experimental method | X-RAY DIFFRACTION (1.6 Å)  | 
Structure validation
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