2DOG
Solution structure of the N-terminal domain of RimM from Thermus thermophilus HB8
Summary for 2DOG
| Entry DOI | 10.2210/pdb2dog/pdb |
| NMR Information | BMRB: 10138 |
| Descriptor | Probable 16S rRNA-processing protein rimM (1 entity in total) |
| Functional Keywords | beta barrel, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, structural genomics, unknown function |
| Biological source | Thermus thermophilus |
| Cellular location | Cytoplasm (By similarity): Q5SJH5 |
| Total number of polymer chains | 1 |
| Total formula weight | 9493.97 |
| Authors | Suzuki, S.,Matsumoto, E.,Tatsuguchi, A.,Kawazoe, M.,Kaminishi, T.,Takemoto, C.,Shirouzu, M.,Muto, Y.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2006-04-28, release date: 2007-04-17, Last modification date: 2024-05-01) |
| Primary citation | Suzuki, S.,Tatsuguchi, A.,Matsumoto, E.,Kawazoe, M.,Kaminishi, T.,Shirouzu, M.,Muto, Y.,Takemoto, C.,Yokoyama, S. Structural characterization of the ribosome maturation protein, RimM J.Bacteriol., 189:6397-6406, 2007 Cited by PubMed Abstract: The RimM protein has been implicated in the maturation of the 30S ribosomal subunit. It binds to ribosomal protein S19, located in the head domain of the 30S subunit. Multiple sequence alignments predicted that RimM possesses two domains in its N- and C-terminal regions. In the present study, we have produced Thermus thermophilus RimM in both the full-length form (162 residues) and its N-terminal fragment, spanning residues 1 to 85, as soluble proteins in Escherichia coli and have performed structural analyses by nuclear magnetic resonance spectroscopy. Residues 1 to 80 of the RimM protein fold into a single structural domain adopting a six-stranded beta-barrel fold. On the other hand, the C-terminal region of RimM (residues 81 to 162) is partly folded in solution. Analyses of 1H-15N heteronuclear single quantum correlation spectra revealed that a wide range of residues in the C-terminal region, as well as the residues in the vicinity of a hydrophobic patch in the N-terminal domain, were dramatically affected upon complex formation with ribosomal protein S19. PubMed: 17616598DOI: 10.1128/JB.00024-07 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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