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Titolo:
Crystal structure of a bifunctional transformylase and cyclohydrolase enzyme in purine biosynthesis
Autore:
Greasley, SE; Horton, P; Ramcharan, J; Beardsley, GP; Benkovic, SJ; Wilson, IA;
Indirizzi:
Scripps Clin & Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA Scripps Clin & Res Inst La Jolla CA USA 92037 iol, La Jolla, CA 92037 USA Scripps Clin & Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA Scripps Clin & Res Inst La Jolla CA USA 92037 iol, La Jolla, CA 92037 USA Penn State Univ, Dept Chem, University Pk, PA 16802 USA Penn State Univ University Pk PA USA 16802 m, University Pk, PA 16802 USA Yale Univ, Sch Med, Dept Pediat, New Haven, CT 06520 USA Yale Univ New Haven CT USA 06520 ed, Dept Pediat, New Haven, CT 06520 USA Yale Univ, Sch Med, Dept Pharmacol, New Haven, CT 06520 USA Yale Univ NewHaven CT USA 06520 Dept Pharmacol, New Haven, CT 06520 USA
Titolo Testata:
NATURE STRUCTURAL BIOLOGY
fascicolo: 5, volume: 8, anno: 2001,
pagine: 402 - 406
SICI:
1072-8368(200105)8:5<402:CSOABT>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI; RIBONUCLEOTIDE TRANSFORMYLASE; 5-AMINOIMIDAZOLE-4-CARBOXAMIDE-RIBONUCLEOTIDE TRANSFORMYLASE; ANTIINFLAMMATORY MECHANISM; NUCLEOTIDE BIOSYNTHESIS; AICAR TRANSFORMYLASE; ANGSTROM RESOLUTION; IMP CYCLOHYDROLASE; ADENOSINE RELEASE; INFLAMED SITES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Wilson, IA Scripps Clin & Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA Scripps Clin & Res Inst La Jolla CA USA 92037 la, CA 92037 USA
Citazione:
S.E. Greasley et al., "Crystal structure of a bifunctional transformylase and cyclohydrolase enzyme in purine biosynthesis", NAT ST BIOL, 8(5), 2001, pp. 402-406

Abstract

ATIC, the product of the purH gene, is a 64 kDa bifunctional enzyme that possesses the final two activities in denovo purine biosynthesis, AICAR transformylase and IMP cyclohydrolase, The crystal structure of avian ATIC has been determined to 1.75 Angstrom resolution by the MAD method using a Se-methionine modified enzyme. ATIC forms an intertwined dimer with an extensiveinterface of similar to5,000 Angstrom (2) per monomer. Each monomer is composed of two novel, separate functional domains. The N-terminal domain (up to residue 199) is responsible for the IMPCH activity, whereas the AICAR Tfase activity resides in the C-terminal domain (200-593). The active sites of the IMPCH and AICAR Tfase domains are similar to 50 Angstrom apart, with no structural evidence of a tunnel connecting the two active sites. The crystal structure of ATIC provides a framework to probe both catalytic mechanisms and to design specific inhibitors for use in cancer chemotherapy and inflammation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/09/20 alle ore 07:10:29