Abstract
The crystal structure of a conserved hypothetical protein from Escherichia coli has been determined using X-ray crystallography. The protein belongs to the Cluster of Orthologous Group COG1553 (National Center for Biotechnology Information database, NLM, NIH), for which there was no structural information available until now. Structural homology search with DALI algorism indicated that this protein has a new fold with no obvious similarity to those of other proteins with known three-dimensional structures. The protein quaternary structure consists of a dimer of trimers, which makes a characteristic cylinder shape. There is a large closed cavity with zn approximate dimensions of 16 Å x 16 Å x 20 Å in the center of the hexameric structure. Six putative active sites are positioned along the equatorial surface of the hexamer. There are several highly conserved residues including two possible functional cysteines in the putative active site. The possible molecular function of the protein is discussed.
| Original language | English |
|---|---|
| Pages (from-to) | 53-66 |
| Number of pages | 14 |
| Journal | Journal of Structural and Functional Genomics |
| Volume | 2 |
| Issue number | 1 |
| DOIs | |
| State | Published - 2002 |
Bibliographical note
Funding Information:We thank Dr Thomas Earnest and Dr Keith Henderson (Advanced Light Source, Lawrence Berkeley National Laboratory) for assistance during data collection at ALS, Dr Weiru Wang and Dr Ed Berry for helpful advice during the structure determination, and Dr Igor Grigoriev for searching the E. coli database. This work was supported by the grants from the Director, Office of Science, Office of Biological and Environmental Research under U.S. Department of Energy (Contract No. DE-AC03-76SF00098) and from National Institutes of Health (P50 GM62412).
Keywords
- Conserved cysteine
- Crystal structure
- Hypothetical protein
- New fold
- Structural genomics