5fr7: Difference between revisions
New page: '''Unreleased structure''' The entry 5fr7 is ON HOLD Authors: Bartho, J.D., Bellini, D., Wuerges, J., Demitri, N., Walsh, M., Benini, S. Description: Erwinia amylovora AmyR amylovoran ... |
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The | ==Erwinia amylovora AmyR amylovoran repressor, a member of the YbjN protein family== | ||
<StructureSection load='5fr7' size='340' side='right'caption='[[5fr7]], [[Resolution|resolution]] 1.95Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5fr7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Erwinia_amylovora_CFBP1430 Erwinia amylovora CFBP1430]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FR7 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]] 1.95Å</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=5fr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fr7 OCA], [https://pdbe.org/5fr7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fr7 RCSB], [https://www.ebi.ac.uk/pdbsum/5fr7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fr7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/D4I047_ERWAC D4I047_ERWAC] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
AmyR is a stress and virulence associated protein from the plant pathogenic Enterobacteriaceae species Erwinia amylovora, and is a functionally conserved ortholog of YbjN from Escherichia coli. The crystal structure of E. amylovora AmyR reveals a class I type III secretion chaperone-like fold, despite the lack of sequence similarity between these two classes of protein and lacking any evidence of a secretion-associated role. The results indicate that AmyR, and YbjN proteins in general, function through protein-protein interactions without any enzymatic action. The YbjN proteins of Enterobacteriaceae show remarkably low sequence similarity with other members of the YbjN protein family in Eubacteria, yet a high level of structural conservation is observed. Across the YbjN protein family sequence conservation is limited to residues stabilising the protein core and dimerization interface, while interacting regions are only conserved between closely related species. This study presents the first structure of a YbjN protein from Enterobacteriaceae, the most highly divergent and well-studied subgroup of YbjN proteins, and an in-depth sequence and structural analysis of this important but poorly understood protein family. | |||
The crystal structure of Erwinia amylovora AmyR, a member of the YbjN protein family, shows similarity to type III secretion chaperones but suggests different cellular functions.,Bartho JD, Bellini D, Wuerges J, Demitri N, Toccafondi M, Schmitt AO, Zhao Y, Walsh MA, Benini S PLoS One. 2017 Apr 20;12(4):e0176049. doi: 10.1371/journal.pone.0176049., eCollection 2017. PMID:28426806<ref>PMID:28426806</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5fr7" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Erwinia amylovora CFBP1430]] | ||
[[Category: Large Structures]] | |||
[[Category: Bartho JD]] | |||
[[Category: Bellini D]] | |||
[[Category: Benini S]] | |||
[[Category: Demitri N]] | |||
[[Category: Walsh M]] | |||
[[Category: Wuerges J]] | |||