The structure of SAV1646 from Staphylococcus aureus belonging to a new `ribosome‐associated' subfamily of bacterial proteins. (1st February 2015)

• Record Type: Journal Article
• Authors: 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.
• Is Part Of: Acta crystallographica. Volume 71:Part 2(2015:Feb.)
• Page Start: 332
• Page End: 337
• Publication Date: 2015-02-01
• Subjects: Biomolecules -- Structure -- Periodicals; Physical biochemistry -- Periodicals; X-ray crystallography -- Periodicals; Crystallography -- Periodicals; 572
• DOI: 10.1107/S1399004714025619
• Languages: English
• ISSNs: 0907-4449

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>The crystal structure of the SAV1646 protein from the pathogenic microorganism <italic>Staphylococcus aureus</italic> 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 <italic>sav1646</italic> 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.</p> </abstract>