3U01
Crystal structure of onconase double mutant C30A/C75A at 1.12 A resolution
Summary for 3U01
| Entry DOI | 10.2210/pdb3u01/pdb |
| Related | 1ONC 1U00 3HG6 3PHN |
| Descriptor | Protein P-30, SULFATE ION, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | alpha/beta protein, ranpirnase, endonuclease, nuclease, hydrolase, antitumor protein |
| Biological source | Rana pipiens (Northern leopard frog) |
| Total number of polymer chains | 1 |
| Total formula weight | 12128.75 |
| Authors | Kurpiewska, K.,Torrent, G.,Ribo, M.,Vilanova, M.,Loch, J.,Lewinski, K. (deposition date: 2011-09-28, release date: 2011-12-21, Last modification date: 2024-11-20) |
| Primary citation | Kurpiewska, K.,Torrent, G.,Ribo, M.,Loch, J.I.,Vilanova, M.,Lewinski, K. Investigating the effects of double mutation C30A/C75A on onconase structure: Studies at atomic resolution. Biopolymers, 101:454-460, 2014 Cited by PubMed Abstract: The structure of onconase C30A/C75A double mutant has been determined at 1.12Å resolution. The structure has high structural homology to other onconase structures. The changes being results of mutation are relatively small, distributed asymmetrically around the two mutated positions, and they are observed not only in the mutation region but expanded to entire molecule. Different conformation of Lys31 side chain that influences the hydrogen bonding network around catalytic triad is probably responsible for lower catalytic efficiency of double mutant. The decrease in thermal stability observed for the onconase variant might be explained by a less dense packing as manifested by the increase of the molecular volume and the solvent accessible surface area. PubMed: 23996687DOI: 10.1002/bip.22403 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.12 Å) |
Structure validation
Download full validation report
