3FI0
Crystal Structure Analysis of B. stearothermophilus Tryptophanyl-tRNA Synthetase Complexed with Tryptophan, AMP, and Inorganic Phosphate
Summary for 3FI0
| Entry DOI | 10.2210/pdb3fi0/pdb |
| Related | 1D2R 1I6K 1I6L 1I6M 1M83 1MAU 1MAW 1MB2 2OV4 3FHJ |
| Descriptor | Tryptophanyl-tRNA synthetase, TRYPTOPHAN, PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | domain rearrangement, aminoacyl-trna synthetase, atp-binding, cytoplasm, ligase, nucleotide-binding, protein biosynthesis, translation |
| Biological source | Bacillus stearothermophilus |
| Cellular location | Cytoplasm: P00953 |
| Total number of polymer chains | 18 |
| Total formula weight | 684479.59 |
| Authors | Laowanapiban, P.,Kapustina, M.,Vonrhein, C.,Delarue, M.,Koehl, P.,Carter Jr., C.W. (deposition date: 2008-12-10, release date: 2009-02-03, Last modification date: 2024-11-20) |
| Primary citation | Laowanapiban, P.,Kapustina, M.,Vonrhein, C.,Delarue, M.,Koehl, P.,Carter, C.W. Independent saturation of three TrpRS subsites generates a partially assembled state similar to those observed in molecular simulations. Proc.Natl.Acad.Sci.Usa, 106:1790-1795, 2009 Cited by PubMed Abstract: Two new crystal structures of Bacillus stearothermophilus tryptophanyl-tRNA synthetase (TrpRS) afford evidence that a closed interdomain hinge angle requires a covalent bond between AMP and an occupant of either pyrophosphate or tryptophan subsite. They also are within experimental error of a cluster of structures observed in a nonequilibrium molecular dynamics simulation showing partial active-site assembly. Further, the highest energy structure in a minimum action pathway computed by using elastic network models for Open and Pretransition state (PreTS) conformations for the fully liganded TrpRS monomer is intermediate between that simulated structure and a partially disassembled structure from a nonequilibrium molecular dynamics trajectory for the unliganded PreTS. These mutual consistencies provide unexpected validation of inferences drawn from molecular simulations. PubMed: 19174517DOI: 10.1073/pnas.0812752106 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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