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PubMed:11290745 JSONTXT 22 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

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.