View source for 5btz


==Structure of the middle domain of lpg1496 from Legionella pneumophila in P212121 space group==
<StructureSection load='5btz' size='340' side='right'caption='[[5btz]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5btz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_ATCC_43290 Legionella pneumophila subsp. pneumophila ATCC 43290]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BTZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BTZ FirstGlance]. <br>
</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'>[https://proteopedia.org/fgij/fg.htm?mol=5btz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5btz OCA], [https://pdbe.org/5btz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5btz RCSB], [https://www.ebi.ac.uk/pdbsum/5btz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5btz ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Pathogenic gram-negative bacteria use specialized secretion systems that translocate bacterial proteins, termed effectors, directly into host cells where they interact with host proteins and biochemical processes for the benefit of the pathogen. Lpg1496 is a previously uncharacterized effector of Legionella pneumophila, the causative agent of Legionnaire's disease. Here, we crystallized three nucleotide-binding domains from lpg1496. The C-terminal domain, which is conserved among the SidE family of effectors, is formed of two largely alpha-helical lobes with a nucleotide-binding cleft. A structural homology search has shown similarity to phosphodiesterases involved in cleavage of cyclic nucleotides. We have also crystallized a novel domain that occurs twice in the N-terminal half of the protein that we term KLAMP domains due to the presence of homologous domains in bacterial histidine kinase-like ATP-binding region-containing proteins and S-adenosylmethionine-dependent methyltransferase proteins. Both KLAMP structures are very similar but selectively bind 3',5'-cAMP and ADP. A co-crystal of the KLAMP1 domain with 3',5'-cAMP reveals the contribution of Tyr61 and Tyr69 that produce pi-stacking interactions with the adenine ring of the nucleotide. Our study provides the first structural insights into two novel nucleotide-binding domains associated with bacterial virulence.

Structure of the Legionella Effector, lpg1496, Suggests a Role in Nucleotide Metabolism.,Wong K, Kozlov G, Zhang Y, Gehring K J Biol Chem. 2015 Aug 20. pii: jbc.M115.671263. PMID:26294765<ref>PMID:26294765</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Legionella pneumophila subsp. pneumophila ATCC 43290]]
[[Category: Gehring K]]
[[Category: Kozlov G]]
[[Category: Wong K]]