2GK3

Cytoplasmic Protein STM3548 from Salmonella typhimurium

Summary for 2GK3

• Entry DOI: 10.2210/pdb2gk3/pdb
• Descriptor: putative cytoplasmic protein, GLYCEROL (3 entities in total)
• Functional Keywords: salmonella typhimurium, stm3548, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, unknown function
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 6
• Total formula weight: 175943.91

Authors

Petrova, T.,Cuff, M.E.,Wu, R.Y.,Holzle, D.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2006-03-31, release date: 2006-05-02, Last modification date: 2024-10-30)

Primary citation

Petrova, T.,Cuff, M.E.,Wu, R.,Kim, Y.,Holzle, D.,Joachimiak, A.
Novel hexamerization motif is discovered in a conserved cytoplasmic protein from Salmonella typhimurium.
J.Struct.Funct.Genom., 8:19-25, 2007

PubMed Abstract: The cytoplasmic protein Stm3548 of unknown function obtained from a strain of Salmonella typhimurium was determined by X-ray crystallography at a resolution of 2.25 A. The asymmetric unit contains a hexamer of structurally identical monomers. The monomer is a globular domain with a long beta-hairpin protrusion that distinguishes this structure. This beta-hairpin occupies a central position in the hexamer, and its residues participate in the majority of interactions between subunits of the hexamer. We suggest that the structure of Stm3548 presents a new hexamerization motif. Because the residues participating in interdomain interactions are highly conserved among close members of protein family DUF1355 and buried solvent accessible area for the hexamer is significant, the hexamer is most likely conserved as well. A light scattering experiment confirmed the presence of hexamer in solution.

PubMed: 17968677
DOI: 10.1007/s10969-007-9028-1

Experimental method

X-RAY DIFFRACTION (2.25 Å)