Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly
- 116 Downloads
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.
KeywordsPF07873 YabP Dsy0195 Sporulation protein Structural genomics NMR
Double electron electron resonance
Green flourescent protein
Northeast structural genomics consortium
Nuclear magnetic resonance spectroscopy
Nuclear overhauser effect
Nuclear overhauser effect spectroscopy
Paramagnetic relaxation enhancement
Root mean square deviation
This work was supported by the National Institute of General Medical Sciences; Grant Number: U54-GM074958. The majority of the data collection was conducted at the Ohio Biomedicine Center of Excellence in Structural Biology and Metabonomics at Miami University. A portion of the NMR experiments was performed in the Environmental Molecular Sciences Laboratory, a national scientific user facility sponsored by the US Department of Energy’s Office of Biological and Environmental Research and located at Pacific Northwest National Laboratory.
- 3.Yang Y, Ramelot TA, McCarrick RM, Ni S, Feldmann EA, Cort JR, Wang H, Ciccosanti C, Jiang M, Janjua H, Acton TB, Xiao R, Everett JK, Montelione GT, Kennedy MA (2010) Combining NMR and EPR methods for homodimer protein structure determination. J Am Chem Soc 132:11910–11913PubMedCrossRefGoogle Scholar
- 6.Acton TB, Xiao R, Anderson S, Aramini J, Buchwald WA, Ciccosanti C, Conover K, Everett J, Hamilton K, Huang YJ, Janjua H, Kornhaber G, Lau J, Lee DY, Liu G, Maglaqui M, Ma L, Mao L, Patel D, Rossi P, Sahdev S, Shastry R, Swapna GV, Tang Y, Tong S, Wang D, Wang H, Zhao L, Montelione GT (2010) Preparation of protein samples for NMR structure, function, and small-molecule screening studies. Methods Enzymol 493:21–60CrossRefGoogle Scholar