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Titolo:
The Crystal Structure of Human Phosphoglucose Isomerase at 1.6 angstrom resolution: Implications for catalytic mechanism, cytokine activity and haemolytic anaemia
Autore:
Read, J; Pearce, J; Li, XC; Muirhead, H; Chirgwin, J; Davies, C;
Indirizzi:
Univ Sussex, Sch Biol Sci, Brighton BN1 9QG, E Sussex, England Univ Sussex Brighton E Sussex England BN1 9QG BN1 9QG, E Sussex, England Univ Bristol, Sch Med Sci, Bristol BS8 1TD, Avon, England Univ Bristol Bristol Avon England BS8 1TD Bristol BS8 1TD, Avon, England Univ Texas, Hlth Sci Ctr, Dept Med, San Antonio, TX 78229 USA Univ Texas San Antonio TX USA 78229 , Dept Med, San Antonio, TX 78229 USA Vet Adm Med Ctr, Res Serv, San Antonio, TX 78229 USA Vet Adm Med Ctr San Antonio TX USA 78229 Serv, San Antonio, TX 78229 USA
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 2, volume: 309, anno: 2001,
pagine: 447 - 463
SICI:
0022-2836(20010601)309:2<447:TCSOHP>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLUCOSE PHOSPHATE ISOMERASE; AUTOCRINE MOTILITY FACTOR; HEMOLYTIC-ANEMIA; GLUCOSE-6-PHOSPHATE ISOMERASE; GLUCOSEPHOSPHATE ISOMERASE; TRIOSEPHOSPHATE ISOMERASE; PHOSPHOHEXOSE ISOMERASE; NEUROTROPHIC FACTOR; FACTOR NEUROLEUKIN; MOLECULAR-CLONING;
Keywords:
aldose-ketose isomerases; neuroleukin; cytokine; haemolytic anaemia; X-ray crystallography;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
70
Recensione:
Indirizzi per estratti:
Indirizzo: Davies, C Med Univ S Carolina, Dept Biochem & Mol Biol, Charleston, SC 29425 USA Med Univ S Carolina Charleston SC USA 29425 eston, SC 29425 USA
Citazione:
J. Read et al., "The Crystal Structure of Human Phosphoglucose Isomerase at 1.6 angstrom resolution: Implications for catalytic mechanism, cytokine activity and haemolytic anaemia", J MOL BIOL, 309(2), 2001, pp. 447-463

Abstract

Phosphoglucose isomerase (PGI) is a multifunctional protein, which, insidethe cell, functions as a housekeeping enzyme of glycolysis and gluconeogenesis and, outside the cell, exerts wholly unrelated cytokine properties. Wehave determined the structure of human PGI to a resolution of 1.6 Angstromusing X-ray crystallography. The structure is highly similar to other PGIs, especially the architecture of the active site. Fortuitous binding of a sulphate molecule from the crystallisation solution has facilitated an accurate description of the substrate phosphate-binding site. Comparison with both native and inhibitor-bound rabbit PCI structures shows that two loops move closer to the active site upon binding inhibitor. Interestingly, the human structure most closely resembles the inhibitor-bound structure, suggesting that binding of the phosphate moiety of the substrate may trigger this conformational change. We suggest a new mechanism for catalysis that uses Glu357 as the base catalyst for the isomerase reaction rather than His388 as proposed previously. The human PGI structure has also provided a detailed framework with which to map mutations associated with non-spherocytic haemolytic anaemia. (C) 2001 Academic Press.

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Documento generato il 29/09/20 alle ore 18:55:09