Backbone resonance assignments of the 42 kDa enzyme arginine kinase in the transition state analogue form

Omar Davulcu, Xiaogang Niu, Lei Brüschweiler-Li, Rafael Brüschweiler, Jack J. Skalicky, Michael S. Chapman

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

Nearly complete backbone resonance assignments for the 357 residue, 42 kDa enzyme arginine kinase in a transition state analogue (TSA) complex are presented. The TSA is a quaternary complex of arginine kinase, MgADP, arginine, and nitrate. About 93 % (320 of 344) of the non-proline backbone amides were assigned using an enzyme enriched with 2H, 13C, and 15N in combination with three enzyme samples prepared with a single 15N-labeled amino acid (K, L, and R). The amide assignments will provide the foundation for investigating the dynamics of arginine kinase when in a TSA complex.

Original languageEnglish (US)
Pages (from-to)335-338
Number of pages4
JournalBiomolecular NMR Assignments
Volume8
Issue number2
DOIs
StatePublished - Oct 1 2014

Keywords

  • Arginine kinase
  • Enzyme dynamics
  • NMR spectroscopy
  • Phosphagen kinase
  • Resonance assignment
  • Transition state analogue

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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