Refinement of the arginine kinase transition-state analogue complex at 1.2 Å resolution

Mechanistic insights

Mohammad S. Yousef, Felcy Fabiola, James L. Gattis, Thayumanasamy Somasundaram, Michael Chapman

Research output: Contribution to journalArticle

60 Citations (Scopus)

Abstract

The transition-state complex of this 42 kDa homologue of creatine kinase has been refined at 1.2 Å resolution. It indicates that precise positioning of substrates and restriction of the active-site motion are important components in catalysis.

Original languageEnglish (US)
Pages (from-to)2009-2017
Number of pages9
JournalActa Crystallographica Section D: Biological Crystallography
Volume58
Issue number12
DOIs
StatePublished - Dec 1 2002
Externally publishedYes

Fingerprint

Arginine Kinase
creatine
Creatine Kinase
Catalysis
positioning
catalysis
Catalytic Domain
constrictions
analogs
Substrates

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

Cite this

Refinement of the arginine kinase transition-state analogue complex at 1.2 Å resolution : Mechanistic insights. / Yousef, Mohammad S.; Fabiola, Felcy; Gattis, James L.; Somasundaram, Thayumanasamy; Chapman, Michael.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 58, No. 12, 01.12.2002, p. 2009-2017.

Research output: Contribution to journalArticle

Yousef, Mohammad S. ; Fabiola, Felcy ; Gattis, James L. ; Somasundaram, Thayumanasamy ; Chapman, Michael. / Refinement of the arginine kinase transition-state analogue complex at 1.2 Å resolution : Mechanistic insights. In: Acta Crystallographica Section D: Biological Crystallography. 2002 ; Vol. 58, No. 12. pp. 2009-2017.
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