1D1R
NMR SOLUTION STRUCTURE OF THE PRODUCT OF THE E. COLI YCIH GENE.
Summary for 1D1R
Entry DOI | 10.2210/pdb1d1r/pdb |
Descriptor | HYPOTHETICAL 11.4 KD PROTEIN YCIH IN PYRF-OSMB INTERGENIC REGION (1 entity in total) |
Functional Keywords | alpha-beta plait, open-faced beta sandwich, ferredoxin-like fold, structural genomics |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 12488.43 |
Authors | Cort, J.R.,Koonin, E.V.,Bash, P.A.,Kennedy, M.A. (deposition date: 1999-09-20, release date: 1999-10-06, Last modification date: 2024-05-22) |
Primary citation | Cort, J.R.,Koonin, E.V.,Bash, P.A.,Kennedy, M.A. A phylogenetic approach to target selection for structural genomics: solution structure of YciH. Nucleic Acids Res., 27:4018-4027, 1999 Cited by PubMed Abstract: Structural genomics presents an enormous challenge with up to 100 000 protein targets in the human genome alone. At current rates of structure deter-mination, judicious selection of targets is necessary. Here, a phylogenetic approach to target selection is described which makes use of the National Center for Biotechnology Information database of Clusters of Orthologous Groups (COGS). The strategy is designed so that each new protein structure is likely to provide novel sequence-fold information. To demonstrate this approach, the NMR solution structure of YciH (COG0023), a putative translation initiation factor from Escherichia coli, has been determined and its fold classified. YciH is an ortholog of eIF-1/SUI1, an integral component of the translation initiation complex in eukaryotes. The structure consists of two antiparallel alpha-helices packed against the same side of a five-stranded beta-sheet. The first 31 residues of the 11.5 kDa protein are unstructured in solution. Comparative analysis indicates that the folded portion of YciH resembles a number of structures with the alpha-beta plait topology, though its sequence is not homologous to any of them. Thus, the phylogenetic approach to target selection described here was used successfully to identify a new homologous superfamily within this topology. PubMed: 10497266DOI: 10.1093/nar/27.20.4018 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
