Solution structure of Mycobacterium tuberculosis adenylate kinase

Structural and Dynamic Studies on Ligand-Free Adenylate Kinase from Mycobacterium tuberculosis Revealed a Closed Conformation that Can Be Related to the Reduced Catalytic Activity.

MRVLLLGPPGAGKGTQAVKLAEKLGIPQISTGELFRRNIEEGTKLGVEAKRYLDAGDLVPSDLTNELVDDRLNNPDAANG
FILDGYPRSVEQAKALHEMLERRGTDIDAVLEFRVSEEVLLERLKGRGRADDTDDVILNRMKVYRDETAPLLEYYRDQLK
TVDAVGTMDEVFARALRALGK

structures with the lowest restraint violations and lowest energy

3D 15N, 13C HNCA, HNCOCA, HNCACB, HNCOCACB, HCCH-TOCSY

the structures are based on a 1809 are NOE-derived distance constraints, 191 dihedral angle restraints,159 distance restraints from hydrogen bonds.

1.2 mM adenylate kinase 15N, 13C, 50mM potassium phosphate buffer pH 7.1

1.0 mM adenylate kinase 50mM potassium phosphate buffer pH 7.1

1.2 mM adenylate kinase 50mM potassium phosphate buffer pH 7.1

1.2 mM adenylate kinase 15N, 50mM potassium phosphate buffer pH 7.1