1JRK
Crystal Structure of a Nudix Protein from Pyrobaculum aerophilum Reveals a Dimer with Intertwined Beta Sheets
Summary for 1JRK
| Entry DOI | 10.2210/pdb1jrk/pdb |
| Related | 1K26 1K2E 1MUT 1TUM |
| Descriptor | Nudix homolog, (4S)-2-METHYL-2,4-PENTANEDIOL (3 entities in total) |
| Functional Keywords | nudix/mutt-like fold, mixed alpha/beta, tetramerization due to hix6x tag, putative nudix hydrolase, structural genomics, unknown function |
| Biological source | Pyrobaculum aerophilum |
| Total number of polymer chains | 4 |
| Total formula weight | 71963.32 |
| Authors | Wang, S.,Mura, C.,Sawaya, M.R.,Cascio, D.,Eisenberg, D. (deposition date: 2001-08-13, release date: 2002-04-03, Last modification date: 2024-04-03) |
| Primary citation | Wang, S.,Mura, C.,Sawaya, M.R.,Cascio, D.,Eisenberg, D. Structure of a Nudix protein from Pyrobaculum aerophilum reveals a dimer with two intersubunit beta-sheets. Acta Crystallogr.,Sect.D, 58:571-578, 2002 Cited by PubMed Abstract: Nudix proteins, formerly called MutT homolog proteins, are a large family of proteins that play an important role in reducing the accumulation of potentially toxic compounds inside the cell. They hydrolyze a wide variety of substrates that are mainly composed of a nucleoside diphosphate linked to some other moiety X and thus are called Nudix hydrolases. Here, the crystal structure of a Nudix hydrolase from the hyperthermophilic archaeon Pyrobaculum aerophilum is reported. The structure was determined by the single-wavelength anomalous scattering method with data collected at the peak anomalous wavelength of an iridium-derivatized crystal. It reveals an extensive dimer interface, with each subunit contributing two strands to the beta-sheet of the other subunit. Individual subunits consist of a mixed highly twisted and curved beta-sheet of 11 beta-strands and two alpha-helices, forming an alpha-beta-alpha sandwich. The conserved Nudix box signature motif, which contains the essential catalytic residues, is located at the first alpha-helix and the beta-strand and loop preceding it. The unusually short connections between secondary-structural elements, together with the dimer form of the structure, are likely to contribute to the thermostability of the P. aerophilum Nudix protein. PubMed: 11914479DOI: 10.1107/S0907444902001191 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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