Crystallization (Comment) | Organism |
---|---|
enzyme in ternary complex with citrate and cofactor NADP+, X-ray diffraction structure determination and analysis at 1.80 A resolution | Thermus thermophilus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
isocitrate + NADP+ | Thermus thermophilus | - |
oxalosuccinate + NADPH + H+ | - |
r | |
oxalosuccinate | Thermus thermophilus | - |
2-oxoglutarate + CO2 | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermus thermophilus | P33197 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
isocitrate + NADP+ | - |
Thermus thermophilus | oxalosuccinate + NADPH + H+ | - |
r | |
additional information | the isocitrate molecule is located at the active site, and interacts with residues at the cleft between the large and small domain. The catalytic triad residues Lys191, Asp248 and Tyr144 are conserved and interact with isocitrate | Thermus thermophilus | ? | - |
? | |
oxalosuccinate | - |
Thermus thermophilus | 2-oxoglutarate + CO2 | - |
r |
Subunits | Comment | Organism |
---|---|---|
More | the overall fold of the enzyme protein is resolved into large domain, small domain and a clasp domain. The monomeric structure reveals also a unique terminal domain involved in dimerization. The overall TtIDH structure exhibits a closed conformation with the conserved catalytic triad residues Tyr144, Asp248, and Lys191. Oligomerization of the protein is determined using interface area and subunitsubunit interactions between protomers | Thermus thermophilus |
Synonyms | Comment | Organism |
---|---|---|
IDH | - |
Thermus thermophilus |
NADP+ dependent isocitrate dehydrogenase | - |
Thermus thermophilus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | binding site structure | Thermus thermophilus | |
NADPH | - |
Thermus thermophilus |
General Information | Comment | Organism |
---|---|---|
evolution | the overall fold of the enzyme protein is resolved into large domain, small domain and a clasp domain. The monomeric structure reveals also a terminal domain involved in dimerization, a very unique domain when compared to other IDHs. The small domain and clasp domain show significant differences when compared to other IDHs of the same subfamily. The structure of TtIDH reveals the absence of helix at the clasp domain, which is mainly involved in oligomerization in other IDHs. Also, helices/beta sheets are absent in the small domain, when compared to other IDHs of the same subfamily. The overall TtIDH structure exhibits a closed conformation with the conserved catalytic triad residues Tyr144, Asp248, and Lys191. Oligomerization of the protein is determined using interface area and subunitsubunit interactions between protomers. The TtIDH structure with the terminal domain may be categorized as a first structure of a type IV subfamily | Thermus thermophilus |