| Autor: |
Chirgadze, Yuri N., Clarke, Teresa E., Romanov, Vladimir, Kisselman, Gera, Wu-Brown, Jean, Soloveychik, Maria, Chan, Tiffany S. Y., Gordon, Roni D., Battaile, Kevin P., Pai, Emil F., Chirgadze, Nickolay Y. |
| Předmět: |
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| Zdroj: |
Acta Crystallographica: Section D (Wiley-Blackwell); Feb2015, Vol. 71 Issue 2, p332-337, 6p |
| Abstrakt: |
The crystal structure of the SAV1646 protein from the pathogenic microorganism Staphylococcus aureus has been determined at 1.7 Å resolution. The 106-amino-acid protein forms a two-layer sandwich with α/β topology. The protein molecules associate as dimers in the crystal and in solution, with the monomers related by a pseudo-twofold rotation axis. A sequence-homology search identified the protein as a member of a new subfamily of yet uncharacterized bacterial `ribosome-associated' proteins with at least 13 members to date. A detailed analysis of the crystal protein structure along with the genomic structure of the operon containing the sav1646 gene allowed a tentative functional model of this protein to be proposed. The SAV1646 dimer is assumed to form a complex with ribosomal proteins L21 and L27 which could help to complete the assembly of the large subunit of the ribosome. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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