8j9b

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'''Unreleased structure'''
 
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The entry 8j9b is ON HOLD
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==LnaB-actin binary complex==
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<StructureSection load='8j9b' size='340' side='right'caption='[[8j9b]], [[Resolution|resolution]] 3.42&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8j9b]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila Legionella pneumophila] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8J9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8J9B FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.42&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8j9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8j9b OCA], [https://pdbe.org/8j9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8j9b RCSB], [https://www.ebi.ac.uk/pdbsum/8j9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8j9b ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A8C6VAB1_NAJNA A0A8C6VAB1_NAJNA]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The intracellular bacterial pathogen Legionella pneumophila modulates host cell functions by secreting multiple effectors with diverse biochemical activities. In particular, effectors of the SidE family interfere with host protein ubiquitination in a process that involves production of phosphoribosyl ubiquitin (PR-Ub). Here, we show that effector LnaB converts PR-Ub into ADP-ribosylated ubiquitin, which is further processed to ADP-ribose and functional ubiquitin by the (ADP-ribosyl)hydrolase MavL, thus maintaining ubiquitin homeostasis in infected cells. Upon being activated by actin, LnaB also undergoes self-AMPylation on tyrosine residues. The activity of LnaB requires a motif consisting of Ser, His and Glu (SHxxxE) present in a large family of toxins from diverse bacterial pathogens. Thus, our study sheds light on the mechanisms by which a pathogen maintains ubiquitin homeostasis and identifies a family of enzymes capable of protein AMPylation.
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Authors: Chen, T.T., Ouyang, S.Y.
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Legionella maintains host cell ubiquitin homeostasis by effectors with unique catalytic mechanisms.,Fu J, Li S, Guan H, Li C, Zhao YB, Chen TT, Xian W, Zhang Z, Liu Y, Guan Q, Wang J, Lu Q, Kang L, Zheng SR, Li J, Cao S, Das C, Liu X, Song L, Ouyang S, Luo ZQ Nat Commun. 2024 Jul 15;15(1):5953. doi: 10.1038/s41467-024-50311-2. PMID:39009586<ref>PMID:39009586</ref>
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Description: LnaB-actin binary complex
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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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[[Category: Chen, T.T]]
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<div class="pdbe-citations 8j9b" style="background-color:#fffaf0;"></div>
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[[Category: Ouyang, S.Y]]
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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: Large Structures]]
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[[Category: Legionella pneumophila]]
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[[Category: Oryctolagus cuniculus]]
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[[Category: Chen TT]]
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[[Category: Ouyang SY]]

Current revision

LnaB-actin binary complex

PDB ID 8j9b

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