4K2J
Decameric ring structure of KSHV (HHV-8) latency-associated nuclear antigen (LANA) DNA binding domain
Summary for 4K2J
| Entry DOI | 10.2210/pdb4k2j/pdb |
| Descriptor | KSHV (HHV-8) latency-associated nuclear antigen (LANA), FORMIC ACID, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | dna binding, dna binding protein, viral protein |
| Biological source | Human herpesvirus 8 (HHV-8) |
| Total number of polymer chains | 10 |
| Total formula weight | 160613.77 |
| Authors | Domsic, J.F.,Marmorstein, R. (deposition date: 2013-04-09, release date: 2013-11-06, Last modification date: 2024-02-28) |
| Primary citation | Domsic, J.F.,Chen, H.S.,Lu, F.,Marmorstein, R.,Lieberman, P.M. Molecular Basis for Oligomeric-DNA Binding and Episome Maintenance by KSHV LANA. Plos Pathog., 9:e1003672-e1003672, 2013 Cited by PubMed Abstract: LANA is the KSHV-encoded terminal repeat binding protein essential for viral replication and episome maintenance during latency. We have determined the X-ray crystal structure of LANA C-terminal DNA binding domain (LANADBD) to reveal its capacity to form a decameric ring with an exterior DNA binding surface. The dimeric core is structurally similar to EBV EBNA1 with an N-terminal arm that regulates DNA binding and is required for replication function. The oligomeric interface between LANA dimers is dispensable for single site DNA binding, but is required for cooperative DNA binding, replication function, and episome maintenance. We also identify a basic patch opposite of the DNA binding surface that is responsible for the interaction with BRD proteins and contributes to episome maintenance function. The structural features of LANADBD suggest a novel mechanism of episome maintenance through DNA-binding induced oligomeric assembly. PubMed: 24146617DOI: 10.1371/journal.ppat.1003672 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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