Functional insights from structural genomics |
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Authors: | Farhad Forouhar Alexandre Kuzin Jayaraman Seetharaman Insun Lee Weihong Zhou Mariam Abashidze Yang Chen Wei Yong Haleema Janjua Yingyi Fang Dongyan Wang Kellie Cunningham Rong Xiao Thomas B Acton Eran Pichersky Daniel F Klessig Carl W Porter Gaetano T Montelione Liang Tong |
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Institution: | (1) Department of Biological Sciences, Northeast Structural Genomics Consortium, Columbia University, New York, NY 10027, USA;(2) Center for Advanced Biotechnology and Medicine, Northeast Structural Genomics Consortium, Rutgers University, Piscataway, NJ 08854, USA;(3) Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI 48109, USA;(4) Boyce Thompson Institute for Plant Research, Tower Road, Ithaca, NY 14853, USA;(5) Department of Pharmacology and Therapeutics, Roswell Park Cancer Institute, Buffalo, NY 14263, USA |
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Abstract: | Structural genomics efforts have produced structural information, either directly or by modeling, for thousands of proteins
over the past few years. While many of these proteins have known functions, a large percentage of them have not been characterized
at the functional level. The structural information has provided valuable functional insights on some of these proteins, through
careful structural analyses, serendipity, and structure-guided functional screening. Some of the success stories based on
structures solved at the Northeast Structural Genomics Consortium (NESG) are reported here. These include a novel methyl salicylate
esterase with important role in plant innate immunity, a novel RNA methyltransferase (H. influenzae yggJ (HI0303)), a novel spermidine/spermine N-acetyltransferase (B. subtilis PaiA), a novel methyltransferase or AdoMet binding protein (A. fulgidus AF_0241), an ATP:cob(I)alamin adenosyltransferase (B. subtilis YvqK), a novel carboxysome pore (E. coli EutN), a proline racemase homolog with a disrupted active site (B. melitensis BME11586), an FMN-dependent enzyme (S. pneumoniae SP_1951), and a 12-stranded β-barrel with a novel fold (V. parahaemolyticus VPA1032). |
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Keywords: | Methyltransferase Spermine Acetyltransferase |
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