We report the solution NMR structure of the 113-residue protein ytfP from Escherichia coli (Swiss-Prot ID: YTFP_ECOLI), target ER111 of the Northeast Structural Genomics Consortium (www.nesg.org). The structure is characterized by a mixed a/b-fold consisting of two helices and eight beta strands. The structure features a large cavity formed by five antiparallel beta strands and the two helices capped by another two strands, as well as an unusual “crossover” of two long beta stranded segments. Comparisons with recent crystal structures of homologues from Pyrococcus horikoshii and Mus musculus reveal that the fold is highly unique to the functionally uncharacterized UPF0131 pfamA protein domain family. The structure expands the modeling leverage coverage of the UPF0131 domain family.
Revised: July 22, 2010 |
Published: May 27, 2007
Citation
Aramini J.M., Y. Huang, G. Swapna, J.R. Cort, P.K. Rajan, R. Xiao, and R. Shastry, et al. 2007.The solution NMR structure of Escherichia coli ytfP expands the structural coverage of the UPF0131 protein domain family.Proteins. Structure, Function, and Bioinformatics 68. PNWD-SA-7702. doi:10.1002/prot.21450