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| | <StructureSection load='5xll' size='340' side='right'caption='[[5xll]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='5xll' size='340' side='right'caption='[[5xll]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5xll]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XLL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XLL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5xll]] 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=5XLL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XLL FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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]] 2.201Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5xll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xll OCA], [http://pdbe.org/5xll PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xll RCSB], [http://www.ebi.ac.uk/pdbsum/5xll PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xll ProSAT]</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=5xll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xll OCA], [https://pdbe.org/5xll PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xll RCSB], [https://www.ebi.ac.uk/pdbsum/5xll PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xll 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: Non-specific serine/threonine protein kinase]] | + | [[Category: Mycobacterium tuberculosis H37Rv]] |
| - | [[Category: Rao, Z]] | + | [[Category: Rao Z]] |
| - | [[Category: Yan, Q]] | + | [[Category: Yan Q]] |
| - | [[Category: Dimer]]
| + | |
| - | [[Category: M. tuberculosis]]
| + | |
| - | [[Category: Pkni]]
| + | |
| - | [[Category: Sensor domain]]
| + | |
| - | [[Category: Transferase]]
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| 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
Protein kinases play central roles in the survival of Mycobacterium tuberculosis within host. Here we report the individual high-resolution crystal structures of the sensor domain (in both monomer and dimer forms) and the kinase domain of PknI, a transmembrane protein member of the serine/threonine protein kinases (STPKs) family. PknI is the first STPK identified whose sensor domain exists in a monomer-dimer equilibrium. Inspection of the two structures of the sensor domain (PknI_SD) revealed conformational changes upon dimerization, with an arm region of critical importance for dimer formation identified. Rapamycin-induced dimerization of unphosphorylated fusions of PknI juxtamembrane and the kinase domain, intended to mimic the dimerization effect presumably imposed by PknI_SD, was observed to be able to activate auto-phosphorylation activity of the kinase domain. In vivo experiments using an M. bovis model suggested PknI functions as a dimer in the regulation of M. tuberculosis growth.
Structural Insight into the Activation of PknI Kinase from M. tuberculosis via Dimerization of the Extracellular Sensor Domain.,Yan Q, Jiang D, Qian L, Zhang Q, Zhang W, Zhou W, Mi K, Guddat L, Yang H, Rao Z Structure. 2017 Aug 1;25(8):1286-1294.e4. doi: 10.1016/j.str.2017.06.010. Epub, 2017 Jul 14. PMID:28712808[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
- ↑ Yan Q, Jiang D, Qian L, Zhang Q, Zhang W, Zhou W, Mi K, Guddat L, Yang H, Rao Z. Structural Insight into the Activation of PknI Kinase from M. tuberculosis via Dimerization of the Extracellular Sensor Domain. Structure. 2017 Aug 1;25(8):1286-1294.e4. doi: 10.1016/j.str.2017.06.010. Epub, 2017 Jul 14. PMID:28712808 doi:http://dx.doi.org/10.1016/j.str.2017.06.010
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