Open Access. Powered by Scholars. Published by Universities.®
Articles 1 - 1 of 1
Full-Text Articles in Entire DC Network
Atomic-Resolution 1.3 Å Crystal Structure, Inhibition By Sulfate, And Molecular Dynamics Of The Bacterial Enzyme Dape, Matthew Kochert, Boguslaw P. Nocek, Thahani S. Habeeb Mohammad, Elliot Gild, Kaitlyn Lovato, Tahirah K. Heath, Richard C. Holz, Kenneth W. Olsen, Daniel P. Becker Ph.D.
Atomic-Resolution 1.3 Å Crystal Structure, Inhibition By Sulfate, And Molecular Dynamics Of The Bacterial Enzyme Dape, Matthew Kochert, Boguslaw P. Nocek, Thahani S. Habeeb Mohammad, Elliot Gild, Kaitlyn Lovato, Tahirah K. Heath, Richard C. Holz, Kenneth W. Olsen, Daniel P. Becker Ph.D.
Chemistry: Faculty Publications and Other Works
We report the atomic-resolution (1.3 Å) X-ray crystal structure of an open conformation of the dapE-encoded N-succinyl-l,l-diaminopimelic acid desuccinylase (DapE, EC 3.5.1.18) from Neisseria meningitidis. This structure [Protein Data Bank (PDB) entry 5UEJ] contains two bound sulfate ions in the active site that mimic the binding of the terminal carboxylates of the N-succinyl-l,l-diaminopimelic acid (l,l-SDAP) substrate. We demonstrated inhibition of DapE by sulfate (IC50 = 13.8 ± 2.8 mM). Comparison with other DapE structures in the PDB demonstrates the flexibility of the interdomain connections of this protein. This high-resolution structure was then utilized as the …