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Published online on October 23, 2007, 10.1073/pnas.0706659104
PNAS | October 30, 2007 | vol. 104 | no. 44 | 17341-17346


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BIOLOGICAL SCIENCES / BIOCHEMISTRY
The prokaryotic Cys2His2 zinc-finger adopts a novel fold as revealed by the NMR structure of Agrobacterium tumefaciens Ros DNA-binding domain

Gaetano Malgieri*, Luigi Russo*, Sabrina Esposito*, Ilaria Baglivo*, Laura Zaccaro{dagger}, Emilia M. Pedone{dagger}, Benedetto Di Blasio*, Carla Isernia*, Paolo V. Pedone*, and Roberto Fattorusso*,{ddagger}

*Dipartimento di Scienze Ambientali, Seconda Università degli Studi di Napoli, Via Vivaldi 43, 81100 Caserta, Italy; and {dagger}Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale delle Ricerche, Via Mezzocannone 16, 80134 Napoli, Italy

Edited by Gary Felsenfeld, National Institutes of Health, Bethesda, MD, and approved September 18, 2007 (received for review July 16, 2007)

The first putative prokaryotic Cys2His2 zinc-finger domain has been identified in the transcriptional regulator Ros from Agrobacterium tumefaciens, indicating that the Cys2His2 zinc-finger domain, originally thought to be confined to the eukaryotic kingdom, could be widespread throughout the living kingdom from eukaryotic, both animal and plant, to prokaryotic. In this article we report the NMR solution structure of Ros DNA-binding domain (Ros87), providing 79 structural characterization of a prokaryotic Cys2His2 zinc-finger domain. The NMR structure of Ros87 shows that the putative prokaryotic Cys2His2 zinc-finger sequence is indeed part of a significantly larger zinc-binding globular domain that possesses a novel protein fold very different from the classical fold reported for the eukaryotic classical zinc-finger. The Ros87 globular domain consists of 58 aa (residues 9–66), is arranged in a betabetabeta{alpha}{alpha} topology, and is stabilized by an extensive 15-residue hydrophobic core. A backbone dynamics study of Ros87, based on 15N R1, 15N R2, and heteronuclear 15N-{1H}-NOE measurements, has further confirmed that the globular domain is uniformly rigid and flanked by two flexible tails. Mapping of the amino acids necessary for the DNA binding onto Ros87 structure reveals the protein surface involved in the DNA recognition mechanism of this new zinc-binding protein domain.

DNA binding proteins | NMR spectroscopy | Ros protein

Author contributions: B.D.B., C.I., P.V.P., and R.F. designed research; G.M., L.R., S.E., I.B., L.Z., E.M.P., C.I., P.V.P., and R.F. performed research; G.M., L.R., S.E., I.B., L.Z., E.M.P., B.D.B., C.I., P.V.P., and R.F. analyzed data; and G.M., L.R., C.I., P.V.P., and R.F. wrote the paper.

The authors declare no conflict of interest.

This article is a PNAS Direct Submission.

Data deposition: The NMR chemical shifts have been deposited in the BioMagResBank, www.bmrb.wisc.edu (accession no. 15373), and the atomic coordinates have been deposited in the Protein Data Bank, www.pdb.org (PDB ID code 2JSP).

This article contains supporting information online at www.pnas.org/cgi/content/full/0706659104/DC1.

{ddagger}To whom correspondence should be addressed. E-mail: roberto.fattorusso{at}unina2.it

© 2007 by The National Academy of Sciences of the USA


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