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| | <StructureSection load='5m06' size='340' side='right'caption='[[5m06]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='5m06' size='340' side='right'caption='[[5m06]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5m06]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5M06 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5M06 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5m06]] 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=5M06 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5M06 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pknI, Rv2914c, MTCY338.02c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></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=5m06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m06 OCA], [https://pdbe.org/5m06 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5m06 RCSB], [https://www.ebi.ac.uk/pdbsum/5m06 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5m06 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5m06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5m06 OCA], [http://pdbe.org/5m06 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5m06 RCSB], [http://www.ebi.ac.uk/pdbsum/5m06 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5m06 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Myctu]] | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Non-specific serine/threonine protein kinase]]
| + | [[Category: Alexandre M]] |
| - | [[Category: Alexandre, M]] | + | [[Category: Alzari PM]] |
| - | [[Category: Alzari, P M]] | + | [[Category: Barilone N]] |
| - | [[Category: Barilone, N]] | + | [[Category: Bellinzoni M]] |
| - | [[Category: Bellinzoni, M]] | + | [[Category: Lisa MN]] |
| - | [[Category: Lisa, M N]] | + | [[Category: Raynal B]] |
| - | [[Category: Raynal, B]] | + | [[Category: Wagner T]] |
| - | [[Category: Wagner, T]] | + | |
| - | [[Category: Kinase]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Signalling]]
| + | |
| - | [[Category: Tuberculosis]]
| + | |
| Structural highlights
Function
PKNI_MYCTU Plays an important role in slowing down the growth of mycobacteria within the infected host.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Gopalaswamy R, Narayanan S, Chen B, Jacobs WR, Av-Gay Y. The serine/threonine protein kinase PknI controls the growth of Mycobacterium tuberculosis upon infection. FEMS Microbiol Lett. 2009 Jun;295(1):23-9. doi: 10.1111/j.1574-6968.2009.01570.x., Epub 2009 Apr 1. PMID:19341393 doi:http://dx.doi.org/10.1111/j.1574-6968.2009.01570.x
- ↑ Lisa MN, Wagner T, Alexandre M, Barilone N, Raynal B, Alzari PM, Bellinzoni M. The crystal structure of PknI from Mycobacterium tuberculosis shows an inactive, pseudokinase-like conformation. FEBS J. 2017 Jan 5. doi: 10.1111/febs.14003. PMID:28054744 doi:http://dx.doi.org/10.1111/febs.14003
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