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Protein Science (2004), 13:1458-1465. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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Solution structure of the hypothetical protein Mth677 from Methanobacterium thermoautotrophicum: A novel {alpha}+{beta} fold

Francisco J. Blanco1, Adelinda Yee2, Ramón Campos-Olivas1, Ángel R. Ortiz3, Demian Devos4, Alfonso Valencia4, Cheryl H. Arrowsmith2 and Manuel Rico5

1 NMR Group, Centro Nacional de Investigaciones Oncológicas, 28029 Madrid, Spain
2 Division of Molecular and Structural Biology, Ontario Cancer Institute, and Department of Medical Physics, University of Toronto, Toronto, Ontario, Canada M5G 2M9
3 Unidad de Bioinformática, Centro de Biología Molecular, Universidad Autónoma de Madrid, Cantoblanco, 28049 Madrid, Spain
4 Centro Nacional de Biotecnología, Consejo Superior Investigaciones Científicas (CSIC), Cantoblanco, 28049 Madrid, Spain
5 Instituto de Química-Física "Rocasolano," Consejo Superior Investigaciones Científicas (CSIC), 28006 Madrid, Spain

(RECEIVED January 9, 2004; FINAL REVISION March 3, 2004; ACCEPTED March 3, 2004)



Abstract

The structure of Mth677, a hypothetical protein from Methanobacterium thermoautotrophicum (Mth), has been determined by using heteronuclear nuclear magnetic resonance (NMR) methods on a double-labeled 15N-13C sample. Mth677 adopts a novel {alpha}+{beta} fold, consisting of two {alpha}-helices (one N terminal and one C terminal) packed on the same side of a central {beta}-hairpin. This structure is likely shared by its three orthologs, detected in three other Archaebacteria. There are no clear features in the sequences of these proteins or in the genome organization of Mth to make a reliable functional assignment to this protein. However, the structural similarity to Escherichia coli MinE, the protein which controls that division occurs at the midcell site, lends support to the proposal that Mth677 might be, in Mth, the counterpart of the topological specificity domain of MinE in E. coli.

Keywords: Methanobacterium thermoautotrophicum; structural genomics; heteronuclear NMR; {alpha}+{beta} new fold; MinE protein; cell division

Abbreviations: COG, cluster of ortholog groups • NOG, nonsupervised orthologous group • HSQC, heteronuclear single quantum correlation • HNHB, 3D NMR experiment directed to detect scalar cross-correlation between the amide and H{beta}{beta}' protons of a given residue.

Reprint requests to: Manuel Rico, Instituto de Química-Física "Rocasolano," CSIC, Serrano 119, 28006 Madrid, Spain; e-mail: mrico{at}iqfr.csic.es; fax: 34-91-5642431.

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04620504.


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