Protein Science
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Published online before print September 30, 2005, 10.1110/ps.051755805
Protein Science (2005), 14:2880-2886. Published by Cold Spring Harbor Laboratory Press. Copyright © 2005 The Protein Society
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
ps.051755805v1
14/11/2880    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Almeida, M. S.
Right arrow Articles by Wüthrich, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Almeida, M. S.
Right arrow Articles by Wüthrich, K.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

PROTEIN STRUCTURE REPORT

NMR structure of the conserved hypothetical protein TM0487 from Thermotoga maritima: Implications for 216 homologous DUF59 proteins

Marcius S. Almeida, Torsten Herrmann1, Wolfgang Peti2, Ian A. Wilson and Kurt Wüthrich

The Scripps Research Institute (TSRI), Department of Molecular Biology and Joint Center for Structural Genomics, La Jolla, California 92037, USA

(RECEIVED August 5, 2005; FINAL REVISION August 5, 2005; ACCEPTED August 10, 2005)

The NMR structure of the conserved hypothetical protein TM0487 from Thermotoga maritima represents an {alpha}/{beta}-topology formed by the regular secondary structures {alpha}1–{beta}1–{beta}2–{alpha}2–{beta}3–{beta}4–{alpha}3– {beta}5–310{alpha}4, with a small anti-parallel {beta}-sheet of {beta}-strands 1 and 2, and a mixed parallel/anti-parallel {beta}-sheet of {beta}-strands 3–5. Similar folds have previously been observed in other proteins, with amino acid sequence identity as low as 3% and a variety of different functions. There are also 216 sequence homologs of TM0487, which all have the signature sequence of domains of unknown function 59 (DUF59), for which no three-dimensional structures have as yet been reported. The TM0487 structure thus presents a platform for homology modeling of this large group of DUF59 proteins. Conserved among most of the DUF59s are 13 hydrophobic residues, which are clustered in the core of TM0487. A putative active site of TM0487 consisting of residues D20, E22, L23, T51, T52, and C55 is conserved in 98 of the 216 DUF59 sequences. Asp20 is buried within the proposed active site without any compensating positive charge, which suggests that its pKa value may be perturbed. Furthermore, the DUF59 family includes ORFs that are part of a conserved chromosomal group of proteins predicted to be involved in Fe–S cluster metabolism.

Keywords: NMR structure determination; Thermotoga maritima; structural genomics; DUF59 proteins

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051755805.


Reprint requests to: Kurt Wüthrich, The Scripps Research Institute, Department of Molecular Biology and Joint Center for Structural Genomics, La Jolla, CA 92037, USA; e-mail: wuthrich{at}scripps.edu; fax: (858) 784-8014.


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


This article has been cited by other articles:


Home page
MicrobiologyHome page
I. C. Sutcliffe, G. W. Black, and D. J. Harrington
Bioinformatic insights into the biosynthesis of the Group B carbohydrate in Streptococcus agalactiae
Microbiology, May 1, 2008; 154(5): 1354 - 1363.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2005 by The Protein Society.