6be0: Difference between revisions
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==AvrA delL154 with IP6, CoA== | |||
<StructureSection load='6be0' size='340' side='right' caption='[[6be0]], [[Resolution|resolution]] 2.44Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6be0]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BE0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BE0 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=IHP:INOSITOL+HEXAKISPHOSPHATE'>IHP</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6be0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6be0 OCA], [http://pdbe.org/6be0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6be0 RCSB], [http://www.ebi.ac.uk/pdbsum/6be0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6be0 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Bacterial effector proteins are essential for the infection and proliferation of pathogenic bacteria through manipulation of host immune response pathways. AvrA is a Salmonella effector belonging to the YopJ family of acetyltransferases, which suppresses c-JUN N-terminal kinase (JNK) signaling in mammals through acetylation of mitogen activated receptor kinase kinase 4/7 (MKK4/7). Interestingly, two paralogues of AvrA exist that differ by only a single internal leucine residue, which when absent (AvrAL140), abrogates the ability to suppress JNK signaling. Here, we present the first crystal structure of a bacterial effector from an animal pathogen, AvrAL140, accompanied by a thorough biophysical characterization of both AvrA variants. The structure in complex with inositol hexaphosphate and coenzyme A reveals two closely associated domains consisting of a catalytic core that resembles the CE clan peptidases, and a wedge-shaped regulatory region that mediates co-factor and substrate binding. The loss of the putative function of AvrAL140 is due to its inability to interact with MKK4/7, which ultimately arises from an altered conformation of a critical helix adjacent to the active site, that harbors L140. These results provide general insights into substrate recognition across the YopJ family of acetyltransferases. | |||
Structural analysis of the bacterial effector, AvrA, identifies a critical helix involved in MKK4-substrate recognition.,Labriola J, Zhou Y, Nagar B Biochemistry. 2018 Jul 19. doi: 10.1021/acs.biochem.8b00512. PMID:30025209<ref>PMID:30025209</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6be0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Labriola, J M]] | |||
[[Category: Nagar, B]] | |||
[[Category: Acetyltransferase]] | |||
[[Category: Bacterial effector]] | |||
[[Category: Ip6]] | |||
[[Category: Transferase]] | |||
[[Category: Yopj family]] | |||
