4QYS
TrpB2 enzymes
Summary for 4QYS
| Entry DOI | 10.2210/pdb4qys/pdb |
| Descriptor | Tryptophan synthase beta chain 2, (5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL DIHYDROGEN PHOSPHATE, PYRIDOXAL-5'-PHOSPHATE, ... (5 entities in total) |
| Functional Keywords | enzyme evolution, functional annotation, tryptophan synthase, lyase |
| Biological source | Sulfolobus solfataricus P2 |
| Total number of polymer chains | 2 |
| Total formula weight | 99394.64 |
| Authors | Busch, F.,Rajendran, C.,Loeffler, P.,Merkl, R.,Sterner, R. (deposition date: 2014-07-25, release date: 2015-02-18, Last modification date: 2024-03-20) |
| Primary citation | Busch, F.,Rajendran, C.,Mayans, O.,Loffler, P.,Merkl, R.,Sterner, R. TrpB2 enzymes are O-phospho-l-serine dependent tryptophan synthases Biochemistry, 53:6078-6083, 2014 Cited by PubMed Abstract: The rapid increase of the number of sequenced genomes asks for the functional annotation of the encoded enzymes. We used a combined computational-structural approach to determine the function of the TrpB2 subgroup of the tryptophan synthase β chain/β chain-like TrpB1-TrpB2 family (IPR023026). The results showed that TrpB2 enzymes are O-phospho-l-serine dependent tryptophan synthases, whereas TrpB1 enzymes catalyze the l-serine dependent synthesis of tryptophan. We found a single residue being responsible for the different substrate specificities of TrpB1 and TrpB2 and confirmed this finding by mutagenesis studies and crystallographic analysis of a TrpB2 enzyme with bound O-phospho-l-serine. PubMed: 25184516DOI: 10.1021/bi500977y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.939 Å) |
Structure validation
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