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1 Department of Chemistry, University at Buffalo, State University of New York, Buffalo, New York 14260, USA
2 Center for Advanced Biotechnology and Medicine and Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey 08854, USA
3 Department of Microbiology and Immunology, Weill Medical College of Cornell University, New York, New York 10021, USA
4 Northeast Structural Genomics Consortium (NEGSC, http://www.nesg.org)
(RECEIVED December 18, 2003; FINAL REVISION January 30, 2004; ACCEPTED February 2, 2004)
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 CX2CX14-16CX2C 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 
-sandwich consisting of two three-stranded sheets with topology B(
), A(
), F(), and C(), D(), E(). 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.
Keywords: RS27_ARCFU; high-throughput NMR; structural genomics; 30S ribosomal protein; zinc finger; Archaeoglobus fulgidis
Reprint requests to: Thomas Szyperski, Department of Chemistry, University of Buffalo, State University of New York, 816 Natural Sciences Complex, Buffalo, NY 14260, USA; e-mail: szypersk{at}chem.buffalo.edu; fax: (716) 645-7338.
Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03589204.
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