6exa: Difference between revisions
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<StructureSection load='6exa' size='340' side='right' caption='[[6exa]], [[Resolution|resolution]] 1.79Å' scene=''> | <StructureSection load='6exa' size='340' side='right' caption='[[6exa]], [[Resolution|resolution]] 1.79Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6exa]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EXA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EXA FirstGlance]. <br> | <table><tr><td colspan='2'>[[6exa]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Legph Legph]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EXA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EXA FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">icmP, lpg0445 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272624 LEGPH])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6exa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6exa OCA], [http://pdbe.org/6exa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6exa RCSB], [http://www.ebi.ac.uk/pdbsum/6exa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6exa ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6exa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6exa OCA], [http://pdbe.org/6exa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6exa RCSB], [http://www.ebi.ac.uk/pdbsum/6exa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6exa ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Legionella pneumophila, a causative agent of pneumonia, utilizes the Type 4B secretion (T4BS) system to translocate over 300 effectors into the host cell during infection. T4BS systems are encoded by a large gene cluster termed dot/icm, three components of which, DotL, DotM, and DotN, form the "coupling complex", which serves as a platform for recruitment of effector proteins. One class of effectors includes proteins containing Glu-rich/E-block sequences at their C terminus. However, the protein or region of the coupling complex mediating recruitment of such effectors is unknown. Here we present the crystal structure of DotM. This all alpha-helical structure exhibits patches of positively charged residues. We show that these regions form binding sites for acidic Glu-rich peptides and that mutants targeting these patches are defective in vivo in the translocation of acidic Glu-rich motif-containing effectors. We conclude that DotM forms the interacting surface for recruitment of acidic Glu-rich motif-containing Legionella effectors. | |||
Legionella DotM structure reveals a role in effector recruiting to the Type 4B secretion system.,Meir A, Chetrit D, Liu L, Roy CR, Waksman G Nat Commun. 2018 Feb 6;9(1):507. doi: 10.1038/s41467-017-02578-x. PMID:29410427<ref>PMID:29410427</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6exa" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Legph]] | |||
[[Category: Meir, A]] | [[Category: Meir, A]] | ||
[[Category: Waksman, G]] | [[Category: Waksman, G]] | ||
Latest revision as of 09:22, 8 March 2018
Crystal structure of DotM cytoplasmic domain (residues 153-380), double mutant R196E/R197ECrystal structure of DotM cytoplasmic domain (residues 153-380), double mutant R196E/R197E
Structural highlights
Publication Abstract from PubMedLegionella pneumophila, a causative agent of pneumonia, utilizes the Type 4B secretion (T4BS) system to translocate over 300 effectors into the host cell during infection. T4BS systems are encoded by a large gene cluster termed dot/icm, three components of which, DotL, DotM, and DotN, form the "coupling complex", which serves as a platform for recruitment of effector proteins. One class of effectors includes proteins containing Glu-rich/E-block sequences at their C terminus. However, the protein or region of the coupling complex mediating recruitment of such effectors is unknown. Here we present the crystal structure of DotM. This all alpha-helical structure exhibits patches of positively charged residues. We show that these regions form binding sites for acidic Glu-rich peptides and that mutants targeting these patches are defective in vivo in the translocation of acidic Glu-rich motif-containing effectors. We conclude that DotM forms the interacting surface for recruitment of acidic Glu-rich motif-containing Legionella effectors. Legionella DotM structure reveals a role in effector recruiting to the Type 4B secretion system.,Meir A, Chetrit D, Liu L, Roy CR, Waksman G Nat Commun. 2018 Feb 6;9(1):507. doi: 10.1038/s41467-017-02578-x. PMID:29410427[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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