5m06

Crystal structure of Mycobacterium tuberculosis PknI kinase domain

spinqualitylabelsall models 5m06, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5m06 is a 2 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Ligands: ADP, CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PKNI_MYCTU Plays an important role in slowing down the growth of mycobacteria within the infected host. Publication Abstract from PubMed 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 eleven 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 remarkably short activation segment lacking a peptide-substrate binding site. Consistently with this observation and similarly to earlier findings for eukaryotic pseudokinases, no kinase activity was detected for the catalytic domain of PknI, against different substrates and in various experimental conditions. Based on these results we conclude that PknI may rely on unconventional mechanism(s) for kinase activity and/or it could play alternative role(s) in mycobacterial signalling. This article is protected by copyright. All rights reserved. The crystal structure of PknI from Mycobacterium tuberculosis shows an inactive, pseudokinase-like conformation.,Lisa MN, Wagner T, Alexandre M, Barilone N, Raynal B, Alzari PM, Bellinzoni M FEBS J. 2017 Jan 5. doi: 10.1111/febs.14003. PMID:28054744 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Serine/threonine protein kinase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA