4K2J: Decameric Ring Structure of Kshv (Hhv-8) Latency-associated Nuclear Antigen (Lana) DNA Binding Domain

Citation:
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.
PDB ID: 4K2JDownload
MMDB ID: 114886
PDB Deposition Date: 2013/4/9
Updated in MMDB: 2013/11
Experimental Method:
x-ray diffraction
Resolution: 2.05  Å
Source Organism:
Similar Structures:
Biological Unit for 4K2J: decameric; determined by author and by software (PISA)
Molecular Components in 4K2J
Label Count Molecule
Proteins (10 molecules)
10
Kshv (Hhv-8) Latency-associated Nuclear Antigen (Lana)
Molecule annotation
Chemicals (32 molecules)
1
9
2
23
* Click molecule labels to explore molecular sequence information.

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