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Volumn 306, Issue 3, 2001, Pages 499-511

A 1.8 Å resolution structure of pig muscle 3-phosphoglycerate kinase with bound MgADP and 3-phosphoglycerate in open conformation: New insight into the role of the nucleotide in domain closure

Author keywords

Domain motion; Nucleotide effect; Phosphoglycerate kinase; Source specificity; X ray structure

Indexed keywords

3 PHOSPHOGLYCERIC ACID; ADENOSINE DIPHOSPHATE; ADENOSINE DIPHOSPHATE MAGNESIUM; GLYCERIC ACID; NUCLEOTIDE; PHOSPHOGLYCERATE KINASE; UNCLASSIFIED DRUG; 3-PHOSPHOGLYCERATE; PHOSPHATE;

EID: 0035936656     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4294     Document Type: Article
Times cited : (59)

References (33)
  • 4
    • 0032584315 scopus 로고    scopus 로고
    • Crystal structures of substrates and products bound to the phosphoglycerate kinase active site reveal the catalytic mechanism
    • (1998) Biochemistry , vol.37 , pp. 4429-4436
    • Bernstein, B.E.1    Hol, W.G.2
  • 27
    • 0032437796 scopus 로고    scopus 로고
    • Sequential domain refolding of pig muscle 3-phosphoglycerate kinase: Kinetic analysis of reactivation
    • (1998) Fold. Des. , vol.3 , pp. 565-575
    • Szilágyi, A.N.1    Vas, M.2
  • 28
    • 0022454691 scopus 로고
    • The phosphate group of 3-phosphoglycerate accounts for conformational changes occurring on binding to 3-phosphoglycerate kinase. Enzyme inhibition and thiol reactivity studies
    • (1986) Eur. J. Biochem. , vol.154 , pp. 643-649
    • Tompa, P.1    Hong, P.T.2    Vas, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.