Modeling of the structure of ribosomal protein L1 from the archaeon Haloarcula marismortui
The halophilic archaeon Haloarcula marismortui proliferates in the Dead Sea at extremely high salt concentrations (higher than 3 M). This is the only archaeon, for which the crystal structure of the ribosomal 50S subunit was determined. However, the structure of the functionally important side protu...
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| Veröffentlicht in: | Crystallography reports 2017-07, Vol.62 (4), p.584-588 |
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| container_title | Crystallography reports |
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| creator | Nevskaya, N. A. Kljashtorny, V. G. Vakhrusheva, A. V. Garber, M. B. Nikonov, S. V. |
| description | The halophilic archaeon Haloarcula marismortui proliferates in the Dead Sea at extremely high salt concentrations (higher than 3 M). This is the only archaeon, for which the crystal structure of the ribosomal 50S subunit was determined. However, the structure of the functionally important side protuberance containing the abnormally negatively charged protein L1 (HmaL1) was not visualized. Attempts to crystallize HmaL1 in the isolated state or as its complex with RNA using normal salt concentrations (≤500 mM) failed. A theoretical model of HmaL1 was built based on the structural data for homologs of the protein L1 from other organisms, and this model was refined by molecular dynamics methods. Analysis of this model showed that the protein HmaL1 can undergo aggregation due to the presence of a cluster of positive charges unique for proteins L1. This cluster is located at the RNA–protein interface, which interferes with the crystallization of HmaL1 and the binding of the latter to RNA. |
| doi_str_mv | 10.1134/S1063774517040137 |
| format | Article |
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Analysis of this model showed that the protein HmaL1 can undergo aggregation due to the presence of a cluster of positive charges unique for proteins L1. 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A theoretical model of HmaL1 was built based on the structural data for homologs of the protein L1 from other organisms, and this model was refined by molecular dynamics methods. Analysis of this model showed that the protein HmaL1 can undergo aggregation due to the presence of a cluster of positive charges unique for proteins L1. 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A.</creatorcontrib><creatorcontrib>Kljashtorny, V. G.</creatorcontrib><creatorcontrib>Vakhrusheva, A. V.</creatorcontrib><creatorcontrib>Garber, M. B.</creatorcontrib><creatorcontrib>Nikonov, S. V.</creatorcontrib><collection>CrossRef</collection><collection>OSTI.GOV</collection><jtitle>Crystallography reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nevskaya, N. A.</au><au>Kljashtorny, V. G.</au><au>Vakhrusheva, A. V.</au><au>Garber, M. B.</au><au>Nikonov, S. V.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Modeling of the structure of ribosomal protein L1 from the archaeon Haloarcula marismortui</atitle><jtitle>Crystallography reports</jtitle><stitle>Crystallogr. Rep</stitle><date>2017-07-01</date><risdate>2017</risdate><volume>62</volume><issue>4</issue><spage>584</spage><epage>588</epage><pages>584-588</pages><issn>1063-7745</issn><eissn>1562-689X</eissn><abstract>The halophilic archaeon Haloarcula marismortui proliferates in the Dead Sea at extremely high salt concentrations (higher than 3 M). This is the only archaeon, for which the crystal structure of the ribosomal 50S subunit was determined. However, the structure of the functionally important side protuberance containing the abnormally negatively charged protein L1 (HmaL1) was not visualized. Attempts to crystallize HmaL1 in the isolated state or as its complex with RNA using normal salt concentrations (≤500 mM) failed. A theoretical model of HmaL1 was built based on the structural data for homologs of the protein L1 from other organisms, and this model was refined by molecular dynamics methods. Analysis of this model showed that the protein HmaL1 can undergo aggregation due to the presence of a cluster of positive charges unique for proteins L1. This cluster is located at the RNA–protein interface, which interferes with the crystallization of HmaL1 and the binding of the latter to RNA.</abstract><cop>Moscow</cop><pub>Pleiades Publishing</pub><doi>10.1134/S1063774517040137</doi><tpages>5</tpages></addata></record> |
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| subjects | AGGLOMERATION Clusters COMPUTERIZED SIMULATION CONCENTRATION RATIO CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY CRYSTAL STRUCTURE CRYSTALLIZATION Crystallography and Scattering Methods DEAD SEA Homology Molecular dynamics MOLECULAR DYNAMICS METHOD Physics Physics and Astronomy PROTEINS Ribonucleic acid RNA SALTS Structure of Macromolecular Compounds |
| title | Modeling of the structure of ribosomal protein L1 from the archaeon Haloarcula marismortui |
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