HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Gaspar, J. A. Articles by Meiering, E. M. Search for Related Content PubMed PubMed Citation Articles by Gaspar, J. A. Articles by Meiering, E. M. Social Bookmarking                   What's this?

PROTEIN STRUCTURE REPORT

A novel member of the YchN-like fold: Solution structure of the hypothetical protein Tm0979 from Thermotoga maritima

¹ Guelph-Waterloo Centre for Graduate Studies in Chemistry and Biochemistry, University of Waterloo, Waterloo, Ontario N2L 3G1, Canada
² Department of Medical Biophysics and Ontario Cancer Institute, University of Toronto, Toronto, Ontario M5G 2M9, Canada

(RECEIVED August 25, 2004; FINAL REVISION August 25, 2004; ACCEPTED August 27, 2004)

We report herein the NMR structure of Tm0979, a structural proteomics target from Thermotoga maritima. The Tm0979 fold consists of four / units, which form a central parallel -sheet with strand order 1234. The first three helices pack toward one face of the sheet and the fourth helix packs against the other face. The protein forms a dimer by adjacent parallel packing of the fourth helices sandwiched between the two -sheets. This fold is very interesting from several points of view. First, it represents the first structure determination for the DsrH family of conserved hypothetical proteins, which are involved in oxidation of intracellular sulfur but have no defined molecular function. Based on structure and sequence analysis, possible functions are discussed. Second, the fold of Tm0979 most closely resembles YchN-like folds; however the proteins that adopt these folds differ in secondary structural elements and quaternary structure. Comparison of these proteins provides insight into possible mechanisms of evolution of quaternary structure through a simple mechanism of hydrophobicity-changing mutations of one or two residues. Third, the Tm0979 fold is found to be similar to flavodoxin-like folds and / barrel proteins, and may provide a link between these very abundant folds and putative ancestral half-barrel proteins.

Keywords: Northeast Structural Genomics Consortium; Thermotoga maritima; DsrH; YchN; protein–protein interaction; protein fold evolution; half-barrel; flavodoxin-like fold

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.041068605.

Reprint requests to: Elizabeth M. Meiering, Guelph-Waterloo Centre for Graduate Studies in Chemistry and Biochemistry, University of Waterloo, Waterloo, Ontario N2L 3G1, Canada; e-mail: meiering{at}uwaterloo.ca; fax: (519) 746-0435.

CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				J. Payandeh, M. Fujihashi, W. Gillon, and E. F. Pai The Crystal Structure of (S)-3-O-Geranylgeranylglyceryl Phosphate Synthase Reveals an Ancient Fold for an Ancient Enzyme J. Biol. Chem., March 3, 2006; 281(9): 6070 - 6078. [Abstract] [Full Text] [PDF]