2ZPU
Crystal Structure of Modified Serine Racemase from S.pombe.
Summary for 2ZPU
| Entry DOI | 10.2210/pdb2zpu/pdb |
| Descriptor | Uncharacterized protein C320.14, MAGNESIUM ION, N-(5'-PHOSPHOPYRIDOXYL)-D-ALANINE, ... (4 entities in total) |
| Functional Keywords | plp-dependent, lyase, pyridoxal phosphate, isomerase |
| Biological source | Schizosaccharomyces pombe (Fission yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 35437.72 |
| Authors | Goto, M. (deposition date: 2008-07-29, release date: 2009-04-28, Last modification date: 2023-11-01) |
| Primary citation | Yamauchi, T.,Goto, M.,Wu, H.Y.,Uo, T.,Yoshimura, T.,Mihara, H.,Kurihara, T.,Miyahara, I.,Hirotsu, K.,Esaki, N. Serine racemase with catalytically active lysinoalanyl residue. J.Biochem., 145:421-424, 2009 Cited by PubMed Abstract: Serine racemase synthesizes d-serine, a physiological agonist of the NMDA receptor in mammalian brains. Schizosaccharomyces pombe produces serine racemase (spSR) that is highly similar to the brain enzyme. Our mass-spectrometric and X-ray studies revealed that spSR is modified with its natural substrate serine. spSR remains partially active even though its essential Lys57 inherently forming a Schiff base with the coenzyme pyridoxal 5'-phosphate is converted to N(6)-(R-2-amino-2-carboxyethyl)-l-lysyl (lysino-d-alanyl) residue. This indicates that the alpha-amino group of the d-alanyl moiety of the lysino-d-alanyl residue serves as a catalytic base in the same manner as the epsilon-amino group of Lys57 of the original spSR. PubMed: 19155267DOI: 10.1093/jb/mvp010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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