View source for 5xlm


==Monomer form of M.tuberculosis PknI sensor domain==
<StructureSection load='5xlm' size='340' side='right'caption='[[5xlm]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xlm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XLM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XLM FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pknI, Rv2914c, MTCY338.02c ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [https://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=5xlm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xlm OCA], [https://pdbe.org/5xlm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xlm RCSB], [https://www.ebi.ac.uk/pdbsum/5xlm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xlm 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 ==
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<ref>PMID:28712808</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xlm" 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: Myctu]]
[[Category: Non-specific serine/threonine protein kinase]]
[[Category: Rao, Z]]
[[Category: Yan, Q]]
[[Category: M tuberculosis]]
[[Category: Monomer]]
[[Category: Pkni]]
[[Category: Sensor domain]]
[[Category: Transferase]]