1mru

From Proteopedia

Revision as of 19:32, 20 November 2007

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

Overview

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.

About this Structure

1MRU is a Single protein structure of sequence from Mycobacterium tuberculosis with MG and AGS as ligands. Full crystallographic information is available from OCA.

Reference

Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases., Young TA, Delagoutte B, Endrizzi JA, Falick AM, Alber T, Nat Struct Biol. 2003 Mar;10(3):168-74. PMID:12548283

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