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

• Published in: PloS one Vol. 9; no. 4; p. 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: Journal Article
• Language: English
• Published: United States Public Library of Science 01-04-2014; Public Library of Science (PLoS)
• 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; Mexico
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0094369

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.