4E1O
Human histidine decarboxylase complex with Histidine methyl ester (HME)
Summary for 4E1O
| Entry DOI | 10.2210/pdb4e1o/pdb |
| Descriptor | Histidine decarboxylase, PYRIDOXAL-5'-PHOSPHATE, HISTIDINE-METHYL-ESTER, ... (4 entities in total) |
| Functional Keywords | histidine decarboxylase, lyase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 6 |
| Total formula weight | 328389.02 |
| Authors | Komori, H.,Nitta, Y.,Ueno, H.,Higuchi, Y. (deposition date: 2012-03-06, release date: 2012-07-18, Last modification date: 2023-11-15) |
| Primary citation | Komori, H.,Nitta, Y.,Ueno, H.,Higuchi, Y. Structural study reveals that Ser-354 determines substrate specificity on human histidine decarboxylase J.Biol.Chem., 287:29175-29183, 2012 Cited by PubMed Abstract: Histamine is an important chemical mediator for a wide variety of physiological reactions. L-histidine decarboxylase (HDC) is the primary enzyme responsible for histamine synthesis and produces histamine from histidine in a one-step reaction. In this study, we determined the crystal structure of human HDC (hHDC) complexed with the inhibitor histidine methyl ester. This structure shows the detailed features of the pyridoxal-5'-phosphate inhibitor adduct (external aldimine) at the active site of HDC. Moreover, a comparison of the structures of hHDC and aromatic L-amino acid (L-DOPA) decarboxylase showed that Ser-354 was a key residue for substrate specificity. The S354G mutation at the active site enlarged the size of the hHDC substrate-binding pocket and resulted in a decreased affinity for histidine, but an acquired ability to bind and act on L-DOPA as a substrate. These data provide insight into the molecular basis of substrate recognition among the group II pyridoxal-5'-phosphate-dependent decarboxylases. PubMed: 22767596DOI: 10.1074/jbc.M112.381897 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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