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The crystal structure of PknI from Mycobacterium tuberculosis shows an inactive, pseudokinase-like conformation.

FEBS J.. 2017; 
LisaMaría-Natalia,WagnerTristan,AlexandreMatthieu,BariloneNathalie,RaynalBertrand,AlzariPedro M,BellinzoniM
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Mutagenesis Services Likewise, plasmids pET28a-PknI_C20A and pET28aPknI_C20S were generated by site directed mutagenesis. Plasmids pET28a-PknI_C20A_R136A, pET28a-PknI_C20A_R136N and pET28a-PknI_C20A_AS-PKA were provided by GenScript (Piscataway, USA) using plasmid pET28a-PknI_C20A as template. Get A Quote

摘要

Eukaryotic-like Ser/Thr protein kinases (ePKs) have been identified in many bacterial species, where they are known to mediate signalling mechanisms that share several features with their eukaryotic counterparts. In Mycobacterium tuberculosis, PknI is one of the 11 predicted ePKs and it has been related to bacterial virulence. In order to better understand the molecular basis of its role in mycobacterial signalling, we solved the crystal structure of the PknI cytoplasmic domain. We found that even though PknI possesses most conserved elements characteristic of Hanks-type kinases, it is degraded in several motifs that are essential for the ePKs catalytic activity. Most notably, PknI presents a remarkab... More

关键词

Ser/Thr kinase,X-ray crystallography,activation segment,signal transduc