View source for 5m07


==Crystal structure of Mycobacterium tuberculosis PknI kinase domain, C20A mutant==
<StructureSection load='5m07' size='340' side='right'caption='[[5m07]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5m07]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M07 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M07 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5m07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m07 OCA], [https://pdbe.org/5m07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m07 RCSB], [https://www.ebi.ac.uk/pdbsum/5m07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m07 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PKNI_MYCTU PKNI_MYCTU] Plays an important role in slowing down the growth of mycobacteria within the infected host.<ref>PMID:19341393</ref> 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:28054744</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5m07" style="background-color:#fffaf0;"></div>

==See Also==
*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Alexandre M]]
[[Category: Alzari PM]]
[[Category: Barilone N]]
[[Category: Bellinzoni M]]
[[Category: Lisa MN]]
[[Category: Raynal B]]
[[Category: Wagner T]]