title: Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
abstract: Protein domain family YabP (PF07873) is a family of small protein domains that are conserved in a wide range of bacteria and involved in spore coat assembly during the process of sporulation. The 62-residue fragment of Dsy0195 from Desulfitobacterium hafniense, which belongs to the YabP family, exists as a homodimer in solution under the conditions used for structure determination using NMR spectroscopy. The structure of the Dsy0195 homodimer contains two identical 62-residue monomeric subunits, each consisting of five anti-parallel beta strands (β1, 23-29; β2, 31-38; β3, 41-46; β4, 49-59; β5, 69-80). The tertiary structure of the Dsy0195 monomer adopts a cylindrical fold composed of two beta sheets. The two monomer subunits fold into a homodimer about a single C2 symmetry axis, with the interface composed of two anti-parallel beta strands, β1-β1' and β5b-β5b', where β5b refers to the C-terminal half of the bent β5 strand, without any domain swapping. Potential functional regions of the Dsy0195 structure were predicted based on conserved sequence analysis. The Dsy0195 structure reported here is the first representative structure from the YabP family.
authors: Department of Chemistry and Biochemistry, Miami University, 701 East High Street, Oxford, OH 45056, USA.
authors: Yunhuang
authors: Y
authors: Yang
authors: Theresa A
authors: TA
authors: Ramelot
authors: John R
authors: JR
authors: Cort
authors: Huang
authors: H
authors: Wang
authors: Colleen
authors: C
authors: Ciccosanti
authors: Mei
authors: M
authors: Jiang
authors: Haleema
authors: H
authors: Janjua
authors: Thomas B
authors: TB
authors: Acton
authors: Rong
authors: R
authors: Xiao
authors: John K
authors: JK
authors: Everett
authors: Gaetano T
authors: GT
authors: Montelione
authors: Michael A
authors: MA
authors: Kennedy
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D045858:Desulfitobacterium / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D017510:Protein Folding; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013171:Spores, Bacterial / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins