3VGZ
Crystal structure of E. coli YncE
Summary for 3VGZ
| Entry DOI | 10.2210/pdb3vgz/pdb |
| Related | 3VH0 |
| Descriptor | Uncharacterized protein YncE (2 entities in total) |
| Functional Keywords | beta-propeller, protein binding |
| Biological source | Escherichia coli |
| Total number of polymer chains | 4 |
| Total formula weight | 155409.84 |
| Authors | Kagawa, W.,Sagawa, T.,Niki, H.,Kurumizaka, H. (deposition date: 2011-08-23, release date: 2011-11-16, Last modification date: 2024-11-20) |
| Primary citation | Kagawa, W.,Sagawa, T.,Niki, H.,Kurumizaka, H. Structural basis for the DNA-binding activity of the bacterial beta-propeller protein YncE Acta Crystallogr.,Sect.D, 67:1045-1053, 2011 Cited by PubMed Abstract: β-Propellers are widely utilized in nature as recognition modules. The well conserved β-propeller fold exhibits a high degree of functional diversity, which is probably accomplished through variations in the surface properties of the proteins. Little is known about the interactions between β-propeller proteins and nucleic acids. In the present study, it has been found that the bacterial β-propeller protein YncE binds to DNA. Crystal structures of YncE in the free form and complexed with DNA revealed that the surface region of YncE corresponding to the `canonical' substrate-binding site forms essential contacts with DNA. A single DNA base within a single-stranded DNA region is trapped in the hydrophobic pocket located within the central channel of the β-propeller protein. These data provide physical evidence for the DNA-binding ability of the previously uncharacterized YncE and also suggest that the `canonical' substrate-binding site may be commonly adapted to facilitate nucleic acid binding in a subset of β-propeller proteins. PubMed: 22120742DOI: 10.1107/S0907444911045033 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
Download full validation report
