4xi1: Difference between revisions
New page: '''Unreleased structure''' The entry 4xi1 is ON HOLD Authors: Stogios, P.J., Quaile, T., Skarina, T., Cuff, M., Di Leo, R., Yim, V., Savchenko, A., Joachimiak, A., Midwest Center for St... |
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==Crystal structure of U-box 2 of LubX / LegU2 / Lpp2887 from Legionella pneumophila str. Paris, wild-type== | |||
<StructureSection load='4xi1' size='340' side='right'caption='[[4xi1]], [[Resolution|resolution]] 2.98Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4xi1]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila_str._Paris Legionella pneumophila str. Paris]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4wz1 4wz1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XI1 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]] 2.983Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</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=4xi1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xi1 OCA], [https://pdbe.org/4xi1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xi1 RCSB], [https://www.ebi.ac.uk/pdbsum/4xi1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xi1 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LUBX_LEGPA LUBX_LEGPA] Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
LubX is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. Despite such unique features as the presence of two U-box motifs and its targeting of another effector SidH, the molecular basis of LubX activity remains poorly understood. Here we show that the N terminus of LubX is able to activate an extended number of ubiquitin-conjugating (E2) enzymes including UBE2W, UBEL6, and all tested members of UBE2D and UBE2E families. Crystal structures of LubX alone and in complex with UBE2D2 revealed drastic molecular diversification between the two U-box domains, with only the N-terminal U-box retaining E2 recognition features typical for its eukaryotic counterparts. Extensive mutagenesis followed by functional screening in a yeast model system captured functionally important LubX residues including Arg121, critical for interactions with SidH. Combined, these data provide a new molecular insight into the function of this unique pathogenic factor. | |||
Molecular Characterization of LubX: Functional Divergence of the U-Box Fold by Legionella pneumophila.,Quaile AT, Urbanus ML, Stogios PJ, Nocek B, Skarina T, Ensminger AW, Savchenko A Structure. 2015 Jun 18. pii: S0969-2126(15)00223-3. doi:, 10.1016/j.str.2015.05.020. PMID:26146184<ref>PMID:26146184</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4xi1" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Legionella pneumophila str. Paris]] | |||
[[Category: Cuff M]] | |||
[[Category: Di Leo R]] | |||
[[Category: Joachimiak A]] | |||
[[Category: Quaile T]] | |||
[[Category: Savchenko A]] | |||
[[Category: Skarina T]] | |||
[[Category: Stogios PJ]] | |||
[[Category: Yim V]] | |||
Latest revision as of 10:45, 27 September 2023
Crystal structure of U-box 2 of LubX / LegU2 / Lpp2887 from Legionella pneumophila str. Paris, wild-typeCrystal structure of U-box 2 of LubX / LegU2 / Lpp2887 from Legionella pneumophila str. Paris, wild-type
Structural highlights
FunctionLUBX_LEGPA Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway (By similarity). Publication Abstract from PubMedLubX is part of the large arsenal of effectors in Legionella pneumophila that are translocated into the host cytosol during infection. Despite such unique features as the presence of two U-box motifs and its targeting of another effector SidH, the molecular basis of LubX activity remains poorly understood. Here we show that the N terminus of LubX is able to activate an extended number of ubiquitin-conjugating (E2) enzymes including UBE2W, UBEL6, and all tested members of UBE2D and UBE2E families. Crystal structures of LubX alone and in complex with UBE2D2 revealed drastic molecular diversification between the two U-box domains, with only the N-terminal U-box retaining E2 recognition features typical for its eukaryotic counterparts. Extensive mutagenesis followed by functional screening in a yeast model system captured functionally important LubX residues including Arg121, critical for interactions with SidH. Combined, these data provide a new molecular insight into the function of this unique pathogenic factor. Molecular Characterization of LubX: Functional Divergence of the U-Box Fold by Legionella pneumophila.,Quaile AT, Urbanus ML, Stogios PJ, Nocek B, Skarina T, Ensminger AW, Savchenko A Structure. 2015 Jun 18. pii: S0969-2126(15)00223-3. doi:, 10.1016/j.str.2015.05.020. PMID:26146184[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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