View source for 4bjn


==Crystal structure of the flax-rust effector AvrM-A==
<StructureSection load='4bjn' size='340' side='right'caption='[[4bjn]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bjn]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Melampsora_lini Melampsora lini]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BJN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BJN 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]] 2.9&#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=4bjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bjn OCA], [https://pdbe.org/4bjn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bjn RCSB], [https://www.ebi.ac.uk/pdbsum/4bjn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bjn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q2MV52_MELLI Q2MV52_MELLI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Fungal and oomycete pathogens cause some of the most devastating diseases in crop plants, and facilitate infection by delivering a large number of effector molecules into the plant cell. AvrM is a secreted effector protein from flax rust (Melampsora lini) that can internalize into plant cells in the absence of the pathogen, binds to phosphoinositides (PIPs), and is recognized directly by the resistance protein M in flax (Linum usitatissimum), resulting in effector-triggered immunity. We determined the crystal structures of two naturally occurring variants of AvrM, AvrM-A and avrM, and both reveal an L-shaped fold consisting of a tandem duplicated four-helix motif, which displays similarity to the WY domain core in oomycete effectors. In the crystals, both AvrM variants form a dimer with an unusual nonglobular shape. Our functional analysis of AvrM reveals that a hydrophobic surface patch conserved between both variants is required for internalization into plant cells, whereas the C-terminal coiled-coil domain mediates interaction with M. AvrM binding to PIPs is dependent on positive surface charges, and mutations that abrogate PIP binding have no significant effect on internalization, suggesting that AvrM binding to PIPs is not essential for transport of AvrM across the plant membrane. The structure of AvrM and the identification of functionally important surface regions advance our understanding of the molecular mechanisms underlying how effectors enter plant cells and how they are detected by the plant immune system.

Structures of the flax-rust effector AvrM reveal insights into the molecular basis of plant-cell entry and effector-triggered immunity.,Ve T, Williams SJ, Catanzariti AM, Rafiqi M, Rahman M, Ellis JG, Hardham AR, Jones DA, Anderson PA, Dodds PN, Kobe B Proc Natl Acad Sci U S A. 2013 Oct 7. PMID:24101475<ref>PMID:24101475</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bjn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Melampsora lini]]
[[Category: Kobe B]]
[[Category: Ve T]]
[[Category: Williams SJ]]