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Titolo:
Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 angstrom - Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase
Autore:
Singh, SK; Matsuno, K; LaPorte, DC; Banaszak, LJ;
Indirizzi:
Univ Minnesota, Dept Biochem Mol Biol & Biophys, Minneapolis, MN 55455 USAUniv Minnesota Minneapolis MN USA 55455 iophys, Minneapolis, MN 55455 USA Tufts Univ, Sch Med, Dept Mol Biol & Microbiol, Boston, MA 02111 USA TuftsUniv Boston MA USA 02111 Mol Biol & Microbiol, Boston, MA 02111 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 28, volume: 276, anno: 2001,
pagine: 26154 - 26163
SICI:
0021-9258(20010713)276:28<26154:CSOBSI>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
DEPENDENT PROTEIN-KINASE; X-RAY-DIFFRACTION; MOLECULAR-DYNAMICS; ACTIVE-SITE; PHOSPHORYLATION; ENZYME; PHOSPHATASE; REFINEMENT; MECHANISM; MAPS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Banaszak, LJ Univ Minnesota, Dept Biochem Mol Biol & Biophys, 6-155 Jackson Hall,321 Church St SE, Minneapolis, MN 55455 USA Univ Minnesota 6-155 Jackson Hall,321 Church St SE Minneapolis MN USA 55455
Citazione:
S.K. Singh et al., "Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 angstrom - Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphatase", J BIOL CHEM, 276(28), 2001, pp. 26154-26163

Abstract

Isocitrate dehydrogenase from Bacillus subtilis (BsIDH) is a member of a family of metal-dependent decarboxylating dehydrogenases, Its crystal structure was solved to 1.55 Angstrom and detailed comparisons with the homologuefrom Escherichia coli (EcIDH), the founding member of this family, were made. Although the two IDHs are structurally similar, there are three notabledifferences between them. First, a mostly nonpolar P-strand and two connecting loops in the small domain of EcIDH are replaced by two polar alpha -helices in BsIDH. Because of a 13-residue insert in this region of BsIDH, these helices protrude over the active site cleft of the opposing monomer, 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 Angstrom. Third, although BsIDH is a homodimer,the two unique crystallographic subunits of BsIDH are not structurally identical. 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. In Escherichia coli, IDH is regulated by reversible phosphorylation by the bifunctional enzyme IDH kinase/phosphatase (IDH-K/P), The site of phosphorylation is Ser(113), which lies deep within the active site crevice. Structural differences between EcIDH and BsIDH may explain disparities in their abilities to act as substrates for IDH-K/P.

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Documento generato il 10/07/20 alle ore 09:35:15