4GDF

A Crystal Structure of SV40 Large T Antigen

Summary for 4GDF

• Entry DOI: 10.2210/pdb4gdf/pdb
• Descriptor: Large T antigen, DNA (32-MER), ZINC ION, ... (5 entities in total)
• Functional Keywords: sv40 large t antigen, dna replication, helicase, primase, hydrolase-dna complex, hydrolase/dna
• Biological source: Simian virus 40 (SV40); More
• Total number of polymer chains: 8
• Total formula weight: 269432.73

Authors

Chang, Y.P.,Xu, M.,Chen, X.S. (deposition date: 2012-07-31, release date: 2013-04-10, Last modification date: 2024-02-28)

Primary citation

Chang, Y.P.,Xu, M.,Machado, A.C.,Yu, X.J.,Rohs, R.,Chen, X.S.
Mechanism of Origin DNA Recognition and Assembly of an Initiator-Helicase Complex by SV40 Large Tumor Antigen.
Cell Rep, 3:1117-1127, 2013

PubMed Abstract: The DNA tumor virus Simian virus 40 (SV40) is a model system for studying eukaryotic replication. SV40 large tumor antigen (LTag) is the initiator/helicase that is essential for genome replication. LTag recognizes and assembles at the viral replication origin. We determined the structure of two multidomain LTag subunits bound to origin DNA. The structure reveals that the origin binding domains (OBDs) and Zn and AAA+ domains are involved in origin recognition and assembly. Notably, the OBDs recognize the origin in an unexpected manner. The histidine residues of the AAA+ domains insert into a narrow minor groove region with enhanced negative electrostatic potential. Computational analysis indicates that this region is intrinsically narrow, demonstrating the role of DNA shape readout in origin recognition. Our results provide important insights into the assembly of the LTag initiator/helicase at the replication origin and suggest that histidine contacts with the minor groove serve as a mechanism of DNA shape readout.

PubMed: 23545501
DOI: 10.1016/j.celrep.2013.03.002

Experimental method

X-RAY DIFFRACTION (2.8 Å)