5C5Z
Crystal structure analysis of c4763, a uropathogenic E. coli-specific protein
Summary for 5C5Z
| Entry DOI | 10.2210/pdb5c5z/pdb |
| Descriptor | Glutamyl-tRNA amidotransferase (2 entities in total) |
| Functional Keywords | ggct-like domain, urea, uropathogenic e. coli, hydrolase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 31265.96 |
| Authors | |
| Primary citation | Kim, H.,Choi, J.,Kim, D.,Kim, K.K. Crystal structure analysis of c4763, a uropathogenic Escherichia coli-specific protein. Acta Crystallogr.,Sect.F, 71:1042-1047, 2015 Cited by PubMed Abstract: Urinary-tract infections (UTIs), which are some of the most common infectious diseases in humans, can cause sepsis and death without proper treatment. Therefore, it is necessary to understand their pathogenicity for proper diagnosis and therapeutics. Uropathogenic Escherichia coli, the major causative agents of UTIs, contain several genes that are absent in nonpathogenic strains and are therefore considered to be relevant to UTI pathogenicity. c4763 is one of the uropathogenic E. coli-specific proteins, but its function is unknown. To investigate the function of c4763 and its possible role in UTI pathogenicity, its crystal structure was determined at a resolution of 1.45 Å by a multiple-wavelength anomalous diffraction method. c4763 is a homodimer with 129 residues in one subunit that contains a GGCT-like domain with five α-helices and seven β-strands. c4763 shows structural similarity to the C-terminal domain of allophanate hydrolase from Kluyveromyces lactis, which is involved in the degradation of urea. These results suggest that c4763 might be involved in the utilization of urea, which is necessary for bacterial survival in the urinary tract. Further biochemical and physiological investigation will elucidate its functional relevance in UTIs. PubMed: 26249697DOI: 10.1107/S2053230X15013035 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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