1UIN
Crystal Structure of Threonine Synthase from Thermus Thermophilus HB8, Trigonal Crystal Form
Summary for 1UIN
| Entry DOI | 10.2210/pdb1uin/pdb |
| Related | 1UIM 1UIQ |
| Descriptor | Threonine Synthase, SULFATE ION, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total) |
| Functional Keywords | plp-dependent enzyme, riken structural genomics/proteomics initiative, rsgi, structural genomics, lyase |
| Biological source | Thermus thermophilus |
| Total number of polymer chains | 2 |
| Total formula weight | 74891.79 |
| Authors | Omi, R.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-07-17, release date: 2003-11-18, Last modification date: 2023-12-27) |
| Primary citation | Omi, R.,Masaru, G.,Miyahara, I.,Mizuguchi, H.,Hayashi, H.,Kagamiyama, H.,Hirotsu, K. Crystal Structures of Threonine Synthase from Thermus thermophilus HB8: Conformational change, substrate recognition, and mechanism. J.BIOL.CHEM., 278:46035-46045, 2003 Cited by PubMed Abstract: Threonine synthase, which is a PLP-dependent enzyme, catalyzes the beta,gamma-replacement reaction of l-homoserine phosphate to yield threonine and inorganic phosphate. The three-dimensional structures of the enzyme from Thermus thermophilus HB8 in its unliganded form and complexed with the substrate analogue 2-amino-5-phosphonopentanoic acid have been determined at 2.15 and 2.0 A resolution, respectively. The complexed form, assigned as an enamine, uncovered the interactions of the cofactor-analogue conjugate with the active site residues. The binding of the substrate analogue induces a large conformational change at the domain level. The small domain rotates by about 25 degrees and approaches the large domain to close the active site. The complicated catalytic process of the enzyme has been elucidated based on the complex structure to reveal the stereochemistry of the reaction and to present the released inorganic phosphate as a possible catalyst to carry a proton to the Cgamma atom of the substrate. PubMed: 12952961DOI: 10.1074/jbc.M308065200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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