The solution structure of ribosomal protein S17E from Methanobacterium thermoautotrophicum: a structural homolog of the FF domain.
The ribosomal protein S17E from the archaeon Methanobacterium thermoautotrophicum is a component of the 30S ribosomal subunit. S17E is a 62-residue protein conserved in archaea and eukaryotes and has no counterparts in bacteria. Mammalian S17E is a phosphoprotein component of eukaryotic ribosomes. Archaeal S17E proteins range from 59 to 79 amino acids, and are about half the length of the eukaryotic homologs which have an additional C-terminal region. Here we report the three-dimensional solution structure of S17E. S17E folds into a small three-helix bundle strikingly similar to the FF domain of human HYPA/FBP11, a novel phosphopeptide-binding fold. S17E bears a conserved positively charged surface acting as a robust scaffold for molecular recognition. The structure of M. thermoautotrophicum S17E provides a template for homology modeling of eukaryotic S17E proteins in the family.
Wu
Bin
B
Division of Cancer Genomics and Proteomics, Ontario Cancer Institute, Toronto, Ontario M5G 2M9, Canada.
Yee
Adelinda
A
Huang
Yuanpeng J
YJ
Ramelot
Theresa A
TA
Cort
John R
JR
Semesi
Anthony
A
Jung
Jin-Won
JW
Lee
Weontae
W
Montelione
Gaetano T
GT
Kennedy
Michael A
MA
Arrowsmith
Cheryl H
CH
D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry*; D001665:Binding Sites; D017014:Methanobacterium; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010748:Phosphopeptides / Q000737:chemistry; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D012269:Ribosomal Proteins / Q000737:chemistry*; D016415:Sequence Alignment; D012996:Solutions; D040681:Structural Homology, Protein
D019843:Archaeal Proteins; D010748:Phosphopeptides; D012269:Ribosomal Proteins; D012996:Solutions