| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-74 |
Sentence |
denotes |
Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 A. |
| T2 |
75-199 |
Sentence |
denotes |
Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase. |
| T3 |
200-330 |
Sentence |
denotes |
Isocitrate dehydrogenase from Bacillus subtilis (BsIDH) is a member of a family of metal-dependent decarboxylating dehydrogenases. |
| T4 |
331-495 |
Sentence |
denotes |
Its crystal structure was solved to 1.55 A and detailed comparisons with the homologue from Escherichia coli (EcIDH), the founding member of this family, were made. |
| T5 |
496-593 |
Sentence |
denotes |
Although the two IDHs are structurally similar, there are three notable differences between them. |
| T6 |
594-734 |
Sentence |
denotes |
First, a mostly nonpolar beta-strand and two connecting loops in the small domain of EcIDH are replaced by two polar alpha-helices in BsIDH. |
| T7 |
735-865 |
Sentence |
denotes |
Because of a 13-residue insert in this region of BsIDH, these helices protrude over the active site cleft of the opposing monomer. |
| T8 |
866-1049 |
Sentence |
denotes |
Second, a coil leading into this cleft, the so-called "phosphorylation" loop, is bent inward in the B. subtilis enzyme, narrowing the entrance to the active site from about 12 to 4 A. |
| T9 |
1050-1169 |
Sentence |
denotes |
Third, although BsIDH is a homodimer, the two unique crystallographic subunits of BsIDH are not structurally identical. |
| T10 |
1170-1365 |
Sentence |
denotes |
The two monomers appear to differ by a domain shift of the large domain relative to the small domain/clasp region, reminiscent of what has been observed in the open/closed conformations of EcIDH. |
| T11 |
1366-1494 |
Sentence |
denotes |
In Escherichia coli, IDH is regulated by reversible phosphorylation by the bifunctional enzyme IDH kinase/phosphatase (IDH-K/P). |
| T12 |
1495-1583 |
Sentence |
denotes |
The site of phosphorylation is Ser(113), which lies deep within the active site crevice. |
| T13 |
1584-1707 |
Sentence |
denotes |
Structural differences between EcIDH and BsIDH may explain disparities in their abilities to act as substrates for IDH-K/P. |
