View source for 5los


==Piriformospora indica PIIN_05872==
<StructureSection load='5los' size='340' side='right'caption='[[5los]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5los]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Serendipita_indica_DSM_11827 Serendipita indica DSM 11827]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LOS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LOS 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5los FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5los OCA], [https://pdbe.org/5los PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5los RCSB], [https://www.ebi.ac.uk/pdbsum/5los PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5los ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G4TKU4_SERID G4TKU4_SERID] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Like pathogens, beneficial endophytic fungi secrete effector proteins to promote plant colonization, for example, through perturbation of host immunity. The genome of the root endophyte Serendipita indica encodes a novel family of highly similar, small alanine- and histidine-rich proteins, whose functions remain unknown. Members of this protein family carry an N-terminal signal peptide and a conserved C-terminal DELD motif. Here we report on the functional characterization of the plant-responsive DELD family protein Dld1 using a combination of structural, biochemical, biophysical and cytological analyses. The crystal structure of Dld1 shows an unusual, monomeric histidine zipper consisting of two antiparallel coiled-coil helices. Similar to other histidine-rich proteins, Dld1 displays varying affinity to different transition metal ions and undergoes metal ion- and pH-dependent unfolding. Transient expression of mCherry-tagged Dld1 in barley leaf and root tissue suggests that Dld1 localizes to the plant cell wall and accumulates at cell wall appositions during fungal penetration. Moreover, recombinant Dld1 enhances barley root colonization by S. indica, and inhibits H2 O2 -mediated radical polymerization of 3,3'-diaminobenzidine. Our data suggest that Dld1 has the potential to enhance micronutrient accessibility for the fungus and to interfere with oxidative stress and reactive oxygen species homeostasis to facilitate host colonization.

A secreted fungal histidine- and alanine-rich protein regulates metal ion homeostasis and oxidative stress.,Nostadt R, Hilbert M, Nizam S, Rovenich H, Wawra S, Martin J, Kupper H, Mijovilovich A, Ursinus A, Langen G, Hartmann MD, Lupas AN, Zuccaro A New Phytol. 2020 Aug;227(4):1174-1188. doi: 10.1111/nph.16606. Epub 2020 May 16. PMID:32285459<ref>PMID:32285459</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5los" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Serendipita indica DSM 11827]]
[[Category: Albrecht R]]
[[Category: Hartmann MD]]
[[Category: Lupas AN]]
[[Category: Martin J]]