5C3U
Crystal structure of a fungal L-serine ammonia-lyase from Rhizomucor miehei
Summary for 5C3U
| Entry DOI | 10.2210/pdb5c3u/pdb |
| Descriptor | L-serine ammonia-lyase, PYRIDOXAL-5'-PHOSPHATE (3 entities in total) |
| Functional Keywords | l-serine ammonia-lyase, beta-family plp dependent enzymes, lyase |
| Biological source | Rhizomucor miehei CAU432 |
| Total number of polymer chains | 1 |
| Total formula weight | 39670.06 |
| Authors | Zhen, Q.,Qiaojuan, Y.,Shaoqing, Y.,Zhengqiang, J. (deposition date: 2015-06-17, release date: 2015-12-09, Last modification date: 2024-01-10) |
| Primary citation | Qin, Z.,Yan, Q.,Ma, Q.,Jiang, Z. Crystal structure and characterization of a novel l-serine ammonia-lyase from Rhizomucor miehei. Biochem.Biophys.Res.Commun., 466:431-437, 2015 Cited by PubMed Abstract: L-serine ammonia-lyase, as a member of the β-family of pyridoxal-5'-phosphate (PLP) dependent enzymes, catalyzes the conversion of L-serine (L-threonine) to pyruvate (α-ketobutyrate) and ammonia. The crystal structure of L-serine ammonia-lyase from Rhizomucor miehei (RmSDH) was solved at 1.76 Å resolution by X-ray diffraction method. The overall structure of RmSDH had the characteristic β-family PLP dependent enzyme fold. It consisted of two distinct domains, both of which show the typical open twisted α/β structure. A PLP cofactor was located in the crevice between the two domains, which was attached to Lys52 by a Schiff-base linkage. Unique residue substitutions (Gly78, Pro79, Ser146, Ser147 and Thr312) were discovered at the catalytic site of RmSDH by comparison of structures of RmSDH and other reported eukaryotic L-serine ammonia-lyases. Optimal pH and temperature of the purified RmSDH were 7.5 and 40 °C, respectively. It was stable in the pH range of 7.0-9.0 and at temperatures below 40 °C. This is the first crystal structure of a fungal L-serine ammonia-lyase. It will be useful to study the catalytic mechanism of β-elimination enzymes and will provide a basis for further enzyme engineering. PubMed: 26367174DOI: 10.1016/j.bbrc.2015.09.043 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.76 Å) |
Structure validation
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