Literature summary extracted from
Goto, M.; Hayashi, H.; Miyahara, I.; Hirotsu, K.; Yoshida, M.; Oikawa, T.
Crystal structures of nonoxidative zinc-dependent 2,6-dihydroxybenzoate (gamma-resorcylate) decarboxylase from Rhizobium sp. strain MTP-10005 (2006), J. Biol. Chem., 281, 34365-34373.
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
4.1.1.103 |
structures of native form, the complex with the true substrate (2,6-dihydroxybenzoate), and the complex with 2,3-dihydroxybenzaldehyde at 1.7-, 1.9-, and 1.7-A resolution, respectively. The enzyme exists as a tetramer, and the subunit consists of one (alphabeta)8 triose-phosphate isomerase-barrel domain with three functional linkers and one C-terminal tail. The native enzyme possesses one Zn2+ ion liganded by Glu8, His10, His164, Asp287, and a water molecule at the active site center. The substrate carboxylate takes the place of the water molecule and is coordinated to the Zn2+ ion. The 2-hydroxy group of the substrate is hydrogen-bonded to Asp287, which forms a triad together with His218 and Glu22 |
Rhizobium sp. |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
4.1.1.103 |
Zn2+ |
the native enzyme possesses one Zn2+ ion liganded by Glu8, His10, His164, Asp287, and a water molecule at the active site center |
Rhizobium sp. |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
4.1.1.103 |
Rhizobium sp. |
Q60GU1 |
- |
- |