Letter to the Editor: H-1, C-13 and N-15 Assignments for the Archaeglobus fulgidis Protein AF2095.
The Human genome project promises to provide an unprecedented wealth of information on cell biology, development, evolution and physiology. Translating this immense increase in genomic information into advances in medicine and human health requires a concerted effort to explore and investigate the structure and molecular activity for the vast amount of proteins in the Human proteome that lack any such explicit experimental information. Structural genomics is providing a means to determine the molecular and cellular function of these proteins by characterizing the complete range of protein folds (Montelione, 2001). By annotating sequence information with a protein structure, it is sometimes possible to decipher the biochemical activity of hypothetical proteins from structural similarity and the conservation of spatial arrangement of active site residues. Homology can often be inferred by structural similarity even in the absence of recognizable sequence similarity, and can sometimes be used to identify functional relationships between distantly related proteins. Determining an experimental structure for each protein in a proteome is currently impractical because of the significant time commitment and resources required by X-ray and NMR. Therefore, the current paradigm of structural genomics is to determine a representative structure for each cluster of homologous protein domain sequences that lack similarity to a protein domain with a known structure. In this manner, comparative modeling using a single experimental structure can provide approximate but useful 3D structural information for an entire protein domain family. The Northeast Structural Genomics Consortium (NESG; www.nesg.org) is a pilot project funded by the National Institutes of Health Protein Structure Initiative, focusing on proteins from eukaryotic model organisms including humans. The thermophillic archaea Archaeglobus fulgidis AF2095 protein is an example of a protein of unknown biological function targeted for structural analysis by NESG. AF2095 belongs to the Pfam family PF01981 - UPF0099, protein domain family of unknown function that has been found in yeast, archaebacteria and eubacteria. AF2095 has been assigned to NESG Cluster ID:17431, a set of fourteen protein sequences with high (> {approx}30%) sequence identity (Liu, 2004). This cluster includes proteins of human, Drosophila, Caenorhabditis elegans, Arabidopsis, yeast, archaeal and eubacterial origin. A total of fifty-six proteins are identified when the analysis is expanded to include all available genomes. Therefore, determining the NMR solution structure of AF2095 can be leveraged to infer 3D structural information for at least an additional fifty-five proteins. Here we report the near complete 1H, 15N, 13CO, and 13C NMR assignments and secondary structure of AF2095. These data provide a basis for determining the solution structure of AF2095, for further investigation of the function of this protein and for providing representative structural and functional information for the protein domain family that includes AF2095.
- Research Organization:
- Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
- Sponsoring Organization:
- USDOE
- DOE Contract Number:
- AC05-76RL01830
- OSTI ID:
- 15020731
- Report Number(s):
- PNWD-SA-6538; TRN: US200521%%243
- Journal Information:
- Journal of Biomolecular NMR, Vol. 30, Issue 1
- Country of Publication:
- United States
- Language:
- English
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