9J6J
HBx fused DDB1 4M mutant
Summary for 9J6J
| Entry DOI | 10.2210/pdb9j6j/pdb |
| EMDB information | 61174 |
| Descriptor | Protein X,DNA damage-binding protein 1 (1 entity in total) |
| Functional Keywords | hbv, complex, viral protein |
| Biological source | Hepatitis B virus More |
| Total number of polymer chains | 1 |
| Total formula weight | 146258.09 |
| Authors | Tanaka, H.,Kita, S.,Sasaki, M.,Maenaka, K.,Machida, S. (deposition date: 2024-08-16, release date: 2025-06-04, Last modification date: 2025-06-25) |
| Primary citation | Tanaka, H.,Diogo Dias, J.,Jay, B.,Kita, S.,Sasaki, M.,Takeda, H.,Kishimoto, N.,Sasaki, S.,Misumi, S.,Mizokami, M.,Neuveut, C.,Sumikama, T.,Shibata, M.,Maenaka, K.,Machida, S. Structural basis of the hepatitis B virus X protein in complex with DDB1. Proc.Natl.Acad.Sci.USA, 122:e2421325122-e2421325122, 2025 Cited by PubMed Abstract: A cure for chronic hepatitis B requires eliminating or permanently silencing covalently closed circular DNA (cccDNA). A pivotal target of this approach is the hepatitis B virus (HBV) X protein (HBx), which is a key factor that promotes transcription from cccDNA. However, the HBx structure remains unsolved. Here, we present the cryoelectron microscopy structure of HBx in complex with DDB1, which is an essential complex for cccDNA transcription. In this structure, hydrophobic interactions within HBx were identified, and mutational analysis highlighted their importance in the HBV life cycle. Our biochemical analysis revealed that the HBx-DDB1 complex directly interacts simultaneously with NSE3, which is a component of the SMC5/6 complex, and Spindlin1. Additionally, HBx-DDB1 complex dynamics were explored via high-speed atomic force microscopy. These findings provide comprehensive insights into the structure and function of HBx in HBV replication. PubMed: 40512786DOI: 10.1073/pnas.2421325122 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.86 Å) |
Structure validation
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