1MRU

Intracellular Ser/Thr protein kinase domain of Mycobacterium tuberculosis PknB.

Summary for 1MRU

• Entry DOI: 10.2210/pdb1mru/pdb
• Descriptor: Probable serine/threonine-protein kinase pknB, MAGNESIUM ION, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER (3 entities in total)
• Functional Keywords: regulatory, atp-recognition, molecular evolution, structural genomics, psi, protein structure initiative, tb structural genomics consortium, tbsgc, transferase
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 2
• Total formula weight: 68181.07

Authors

Young, T.A.,Delagoutte, B.,Endrizzi, J.A.,Alber, T.,TB Structural Genomics Consortium (TBSGC) (deposition date: 2002-09-18, release date: 2003-02-11, Last modification date: 2024-02-14)

Primary citation

Young, T.A.,Delagoutte, B.,Endrizzi, J.A.,Falick, A.M.,Alber, T.
Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases.
Nat.Struct.Biol., 10:168-174, 2003

PubMed Abstract: A family of eukaryotic-like Ser/Thr protein kinases occurs in bacteria, but little is known about the structures and functions of these proteins. Here we characterize PknB, a transmembrane signaling kinase from Mycobacterium tuberculosis. The intracellular PknB kinase domain is active autonomously, and the active enzyme is phosphorylated on residues homologous to regulatory phospho-acceptors in eukaryotic Ser/Thr kinases. The crystal structure of the PknB kinase domain in complex with an ATP analog reveals the active conformation. The predicted fold of the PknB extracellular domain matches the proposed targeting domain of penicillin-binding protein 2x. The structural and chemical similarities of PknB to metazoan homologs support a universal activation mechanism of Ser/Thr protein kinases in prokaryotes and eukaryotes.

PubMed: 12548283
DOI: 10.1038/nsb897

Experimental method

X-RAY DIFFRACTION (3 Å)