In:
Acta Crystallographica Section D Biological Crystallography, International Union of Crystallography (IUCr), Vol. 71, No. 2 ( 2015-02-01), p. 332-337
Abstract:
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.
Type of Medium:
Online Resource
ISSN:
1399-0047
DOI:
10.1107/S1399004714025619
Language:
Unknown
Publisher:
International Union of Crystallography (IUCr)
Publication Date:
2015
detail.hit.zdb_id:
2020492-9
detail.hit.zdb_id:
2968623-4
