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...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2014-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3984155?pdf=render |
| _version_ | 1818244817037033472 |
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| author | Jesus S Carrasco-Miranda Alonso A Lopez-Zavala Aldo A Arvizu-Flores Karina D Garcia-Orozco Vivian Stojanoff Enrique Rudiño-Piñera Luis G Brieba Rogerio R Sotelo-Mundo |
| author_facet | Jesus S Carrasco-Miranda Alonso A Lopez-Zavala Aldo A Arvizu-Flores Karina D Garcia-Orozco Vivian Stojanoff Enrique Rudiño-Piñera Luis G Brieba Rogerio R Sotelo-Mundo |
| author_sort | Jesus S Carrasco-Miranda |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-12T14:23:02Z |
| format | Article |
| id | doaj.art-d5d5e19beff64d6abf08b92fa0de643f |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-12T14:23:02Z |
| publishDate | 2014-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-d5d5e19beff64d6abf08b92fa0de643f2022-12-22T00:21:45ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0194e9436910.1371/journal.pone.0094369Crystal structure of the shrimp proliferating cell nuclear antigen: structural complementarity with WSSV DNA polymerase PIP-box.Jesus S Carrasco-MirandaAlonso A Lopez-ZavalaAldo A Arvizu-FloresKarina D Garcia-OrozcoVivian StojanoffEnrique Rudiño-PiñeraLuis G BriebaRogerio R Sotelo-MundoDNA 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.http://europepmc.org/articles/PMC3984155?pdf=render |
| spellingShingle | Jesus S Carrasco-Miranda Alonso A Lopez-Zavala Aldo A Arvizu-Flores Karina D Garcia-Orozco Vivian Stojanoff Enrique Rudiño-Piñera Luis G Brieba Rogerio R Sotelo-Mundo Crystal structure of the shrimp proliferating cell nuclear antigen: structural complementarity with WSSV DNA polymerase PIP-box. PLoS ONE |
| title | Crystal structure of the shrimp proliferating cell nuclear antigen: structural complementarity with WSSV DNA polymerase PIP-box. |
| title_full | Crystal structure of the shrimp proliferating cell nuclear antigen: structural complementarity with WSSV DNA polymerase PIP-box. |
| title_fullStr | Crystal structure of the shrimp proliferating cell nuclear antigen: structural complementarity with WSSV DNA polymerase PIP-box. |
| title_full_unstemmed | Crystal structure of the shrimp proliferating cell nuclear antigen: structural complementarity with WSSV DNA polymerase PIP-box. |
| title_short | Crystal structure of the shrimp proliferating cell nuclear antigen: structural complementarity with WSSV DNA polymerase PIP-box. |
| title_sort | crystal structure of the shrimp proliferating cell nuclear antigen structural complementarity with wssv dna polymerase pip box |
| url | http://europepmc.org/articles/PMC3984155?pdf=render |
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