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6exd

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'''Unreleased structure'''
 
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The entry 6exd is ON HOLD
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==Crystal structure of DotM cytoplasmic domain (residues 153-380) SeMet derivative==
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<StructureSection load='6exd' size='340' side='right' caption='[[6exd]], [[Resolution|resolution]] 2.14&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6exd]] 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=6EXD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EXD FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<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>
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<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=6exd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6exd OCA], [http://pdbe.org/6exd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6exd RCSB], [http://www.ebi.ac.uk/pdbsum/6exd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6exd ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6exd" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Legph]]
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[[Category: Meir, A]]
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[[Category: Waksman, G]]
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[[Category: Legionella pneumophila]]
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[[Category: Membrane protein]]
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[[Category: Protein binding]]
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[[Category: Secretion system]]
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[[Category: Type 4 secretion system]]

Current revision

Crystal structure of DotM cytoplasmic domain (residues 153-380) SeMet derivative

6exd, resolution 2.14Å

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