View source for 5ckw


==Crystal structure of LegK4_AMPPNP Kinase==
<StructureSection load='5ckw' size='340' side='right'caption='[[5ckw]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ckw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila_str._Lens Legionella pneumophila str. Lens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CKW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CKW 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]] 2.49&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5ckw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ckw OCA], [https://pdbe.org/5ckw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ckw RCSB], [https://www.ebi.ac.uk/pdbsum/5ckw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ckw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5WZW9_LEGPL Q5WZW9_LEGPL] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial pathogens subvert signalling pathways to promote invasion and/or replication into the host. LegK1-4 proteins are eukaryotic-like serine/threonine kinases that are translocated by the Dot/Icm type IV secretion system (T4SS) of several Legionella pneumophila strains. We present the crystal structures of an active fragment of the LegK4 protein in apo and substrate-bound states. The structure of LegK4(1-445) reveals a eukaryotic-like kinase domain flanked by a novel cap domain and a four-helix bundle. The protein self-assembles through interactions mediated by helices alphaF and alphaG that generate a dimeric interface not previously observed in a protein kinase. The helix alphaG is displaced compared to previous kinase structures, and its role in stabilization of the activation loop is taken on by the dimerisation interface. The apo-form of the protein has an open conformation with a disordered P-loop but a structured activation segment in absence of targeted phosphorylation. The nucleotide-binding site of LegK4 contains an unusual set of residues that mediate non-canonical interactions with AMP-PNP. Nucleotide binding results in limited changes in the active site, suggesting that LegK4 constitutive kinase activity does not depend on phosphorylation of the activation loop but on the stabilizing effects of the dimer.

The structure of Legionella pneumophila LegK4 type four secretion system (T4SS) effector reveals a novel dimeric eukaryotic-like kinase.,Flayhan A, Berge C, Bailo N, Doublet P, Bayliss R, Terradot L Sci Rep. 2015 Sep 30;5:14602. doi: 10.1038/srep14602. PMID:26419332<ref>PMID:26419332</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ckw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Legionella pneumophila str. Lens]]
[[Category: Flayhan A]]
[[Category: Terradot L]]