Crystal structure of the shrimp proliferating cell nuclear antigen: structural complementarity with WSSV DNA polymerase PIP-box

DNA replication requires processivity factors that allow replicative DNA polymerases to extend long stretches of DNA. Some DNA viruses encode their own replicative DNA polymerase, such as the white spot syndrome virus (WSSV) that infects decapod crustaceans but still require host replication accesso...

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Bibliographic Details
Published in:PloS one 2014-04, Vol.9 (4), p.e94369-e94369
Main Authors: Carrasco-Miranda, Jesus S, Lopez-Zavala, Alonso A, Arvizu-Flores, Aldo A, Garcia-Orozco, Karina D, Stojanoff, Vivian, Rudiño-Piñera, Enrique, Brieba, Luis G, Sotelo-Mundo, Rogerio R
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Analysis
Animals
Antigens
Biochemistry
Biology
Biology and life sciences
Cell cycle
Complementarity
Crustaceans
Crystal structure
Crystallography
Crystallography, X-Ray
Crystals
Data collection
Decapoda
Deoxyribonucleic acid
Diffraction
DNA
DNA biosynthesis
DNA polymerase
DNA polymerases
DNA repair
DNA replication
DNA viruses
DNA-directed DNA polymerase
DNA-Directed DNA Polymerase - chemistry
DNA-Directed DNA Polymerase - metabolism
Gene expression
Genomes
Laboratories
MATERIALS SCIENCE
Molecular Docking Simulation
Molecular Sequence Data
Penaeidae - enzymology
Peptides - metabolism
Physical Sciences
Physiology
Proliferating cell nuclear antigen
Proliferating Cell Nuclear Antigen - chemistry
Proliferating Cell Nuclear Antigen - metabolism
Protein Binding
Protein structure
Proteins
Replication
Sequence Alignment
Static Electricity
Structural Homology, Protein
Structure
Symmetry
Viral infections
Viruses
White spot syndrome
White spot syndrome virus 1 - enzymology
X-ray diffraction
X-rays
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Summary:DNA replication requires processivity factors that allow replicative DNA polymerases to extend long stretches of DNA. Some DNA viruses encode their own replicative DNA polymerase, such as the white spot syndrome virus (WSSV) that infects decapod crustaceans but still require host replication accessory factors. We have determined by X-ray diffraction the three-dimensional structure of the Pacific white leg shrimp Litopenaeus vannamei Proliferating Cell Nuclear Antigen (LvPCNA). This protein is a member of the sliding clamp family of proteins, that binds DNA replication and DNA repair proteins through a motif called PIP-box (PCNA-Interacting Protein). The crystal structure of LvPCNA was refined to a resolution of 3 Å, and allowed us to determine the trimeric protein assembly and details of the interactions between PCNA and the DNA. To address the possible interaction between LvPCNA and the viral DNA polymerase, we docked a theoretical model of a PIP-box peptide from the WSSV DNA polymerase within LvPCNA crystal structure. The theoretical model depicts a feasible model of interaction between both proteins. The crystal structure of shrimp PCNA allows us to further understand the mechanisms of DNA replication processivity factors in non-model systems.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0094369