View source for 6avy


==Crystal structure of Zea mays acyl-protein thioesterase 2==
<StructureSection load='6avy' size='340' side='right'caption='[[6avy]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6avy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Zea_mays Zea mays]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AVY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AVY 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]] 2.24&#8491;</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=6avy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6avy OCA], [https://pdbe.org/6avy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6avy RCSB], [https://www.ebi.ac.uk/pdbsum/6avy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6avy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B6T1C9_MAIZE B6T1C9_MAIZE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Several Pseudomonas and Xanthomonas species are plant pathogens that infect the model organism Arabidopsis thaliana and important crops such as Brassica. Resistant plants contain the infection by rapid cell death of the infected area through the hypersensitive response (HR). A family of highly related alpha/beta hydrolases is involved in diverse processes in all domains of life. Functional details of their catalytic machinery, however, remained unclear. We report the crystal structures of alpha/beta hydrolases representing two different clades of the family, including the protein SOBER1, which suppresses AvrBsT-incited HR in Arabidopsis. Our results reveal a unique hydrophobic anchor mechanism that defines a previously unknown family of protein deacetylases. Furthermore, this study identifies a lid-loop as general feature for substrate turnover in acyl-protein thioesterases and the described family of deacetylases. Furthermore, we found that SOBER1's biological function is not restricted to Arabidopsis thaliana and not limited to suppress HR induced by AvrBsT.

A hydrophobic anchor mechanism defines a deacetylase family that suppresses host response against YopJ effectors.,Burger M, Willige BC, Chory J Nat Commun. 2017 Dec 19;8(1):2201. doi: 10.1038/s41467-017-02347-w. PMID:29259199<ref>PMID:29259199</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6avy" style="background-color:#fffaf0;"></div>

==See Also==
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Zea mays]]
[[Category: Burger M]]
[[Category: Chory J]]
[[Category: Willige BC]]