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 Christendat, D. Articles by Edwards, A. M. Search for Related Content PubMed PubMed Citation Articles by Christendat, D. Articles by Edwards, A. M. Social Bookmarking                   What's this?

The crystal structure of hypothetical protein MTH1491 from Methanobacterium thermoautotrophicum

¹ Clinical Genomics Center, University Health Network, Toronto, Ontario, M5G 1L7, Canada
² Division of Molecular and Structural Biology, Ontario Cancer Institute, Toronto, Ontario, M5G 2M9, Canada
³ Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario, M5G 1L6, Canada
⁴ Biosciences Division and Structural Biology Center, Argonne National Laboratory, Argonne, Illinois 60439, USA

Reprint requests to: Dinesh Christendat, Clinical Genomics Center, University Health Network, 101 College Street, Toronto, Ontario, M5G 1L7, Canada; e-mail: dinesh{at}uhnres.utoronto.ca; fax : (416) 340-4004.

As part of our structural proteomics initiative, we have determined the crystal structure of MTH1491, a previously uncharacterized hypothetical protein from Methanobacterium thermoautotrophicum. MTH1491 is one of numerous structural genomics targets selected in a genome-wide survey of uncharacterized proteins. It belongs to a family of proteins whose biological function is not known. The crystal structure of MTH1491, the first structure for this family of proteins, consists of an overall five-stranded parallel ß-sheet with strand order 51234 and flanking helices. The oligomeric form of this molecule is a trimer as seen from both crystal contacts and gel filtration studies. Analysis revealed that the structure of MTH1491 is similar to that of dehydrogenases, amidohydrolases, and oxidoreductases. Using a combination of sequence and structural analyses, we showed that MTH1491 does not belong to either the dehydrogenase or the amidohydrolase superfamilies of proteins.

Keywords: Hypothetical protein; structural proteomics; X-ray crystallography; structural biology

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

This article has been cited by other articles:

				C. Dahl, S. Engels, A. S. Pott-Sperling, A. Schulte, J. Sander, Y. Lubbe, O. Deuster, and D. C. Brune Novel Genes of the dsr Gene Cluster and Evidence for Close Interaction of Dsr Proteins during Sulfur Oxidation in the Phototrophic Sulfur Bacterium Allochromatium vinosum J. Bacteriol., February 15, 2005; 187(4): 1392 - 1404. [Abstract] [Full Text] [PDF]

				J. A. Gaspar, C. Liu, K. A. Vassall, G. Meglei, R. Stephen, P. B. Stathopulos, A. Pineda-Lucena, B. Wu, A. Yee, C. H. Arrowsmith, et al. A novel member of the YchN-like fold: Solution structure of the hypothetical protein Tm0979 from Thermotoga maritima Protein Sci., January 1, 2005; 14(1): 216 - 223. [Abstract] [Full Text] [PDF]