title: The NMR solution structure of the 30S ribosomal protein S27e encoded in gene RS27_ARCFU of Archaeoglobus fulgidis reveals a novel protein fold.
abstract: The Archaeoglobus fulgidis gene RS27_ARCFU encodes the 30S ribosomal protein S27e. Here, we present the high-quality NMR solution structure of this archaeal protein, which comprises a C4 zinc finger motif of the CX(2)CX(14-16)CX(2)C class. S27e was selected as a target of the Northeast Structural Genomics Consortium (target ID: GR2), and its three-dimensional structure is the first representative of a family of more than 116 homologous proteins occurring in eukaryotic and archaeal cells. As a salient feature of its molecular architecture, S27e exhibits a beta-sandwich consisting of two three-stranded sheets with topology B(decreasing), A(increasing), F(decreasing), and C(increasing), D(decreasing), E(increasing). Due to the uniqueness of the arrangement of the strands, the resulting fold was found to be novel. Residues that are highly conserved among the S27 proteins allowed identification of a structural motif of putative functional importance; a conserved hydrophobic patch may well play a pivotal role for functioning of S27 proteins, be it in archaeal or eukaryotic cells. The structure of human S27, which possesses a 26-residue amino-terminal extension when compared with the archaeal S27e, was modeled on the basis of two structural templates, S27e for the carboxy-terminal core and the amino-terminal segment of the archaeal ribosomal protein L37Ae for the extension. Remarkably, the electrostatic surface properties of archaeal and human proteins are predicted to be entirely different, pointing at either functional variations among archaeal and eukaryotic S27 proteins, or, assuming that the function remained invariant, to a concerted evolutionary change of the surface potential of proteins interacting with S27.
authors.affiliation: Department of Chemistry, University of Buffalo, State University of New York, Buffalo, New York 14260, USA.
authors.forename: Catherine
authors.initials: C
authors.lastname: Herve du Penhoat
authors.forename: Hanudatta S
authors.initials: HS
authors.lastname: Atreya
authors.forename: Yang
authors.initials: Y
authors.lastname: Shen
authors.forename: Gaohua
authors.initials: G
authors.lastname: Liu
authors.forename: Thomas B
authors.initials: TB
authors.lastname: Acton
authors.forename: Rong
authors.initials: R
authors.lastname: Xiao
authors.forename: Zhaohui
authors.initials: Z
authors.lastname: Li
authors.forename: Diana
authors.initials: D
authors.lastname: Murray
authors.forename: Gaetano T
authors.initials: GT
authors.lastname: Montelione
authors.forename: Thomas
authors.initials: T
authors.lastname: Szyperski
mesh_terms: D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000032:analysis / Q000737:chemistry* / Q000235:genetics; D019611:Archaeoglobus fulgidus / Q000235:genetics*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D017510:Protein Folding; D012269:Ribosomal Proteins / Q000032:analysis / Q000737:chemistry* / Q000235:genetics; D016415:Sequence Alignment; D040681:Structural Homology, Protein; D016335:Zinc Fingers
chemical_list: D019843:Archaeal Proteins; D012269:Ribosomal Proteins