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5k34

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Structure of the ankyrin domain of AnkB from Legionella Pneumophila

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Retrieved from "http://52.214.119.220/wiki/index.php/5k34"

Categories: Large Structures | Legionella pneumophila | Gehring K | Kozlov G | Wong K

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 <StructureSection load='5k34' size='340' side='right'caption='[[5k34]], [[Resolution|resolution]] 1.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5k34]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33152 Atcc 33152]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K34 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K34 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5k34]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila Legionella pneumophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5K34 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K34 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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.15&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5k35|5k35]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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">ankB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=446 ATCC 33152])</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=5k34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k34 OCA], [https://pdbe.org/5k34 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k34 RCSB], [https://www.ebi.ac.uk/pdbsum/5k34 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k34 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=5k34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k34 OCA], [http://pdbe.org/5k34 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k34 RCSB], [http://www.ebi.ac.uk/pdbsum/5k34 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k34 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/Q5ZTL7_LEGPH Q5ZTL7_LEGPH]
-Ankyrin B (AnkB/LegAU13) is a translocated F box effector essential for the intracellular replication of the pathogen Legionella pneumophila. AnkB co-opts a host ubiquitin ligase to decorate the pathogen-containing vacuole with K48-linked polyubiquitinated proteins and degrade host proteins as a source of energy. Here, we report that AnkB commandeers the host ubiquitin-proteasome system through mimicry of two eukaryotic protein domains. Using X-ray crystallography, we determined the 3D structure of AnkB in complex with Skp1, a component of the human SCF ubiquitination ligase. The structure confirms that AnkB contains an N-terminal F box similar to Skp2 and a C-terminal substrate-binding domain similar to eukaryotic ankyrin repeats. We identified crucial amino acids in the substrate-binding domain of AnkB and showed them to be essential for the function of AnkB in L. pneumophila intracellular proliferation. The study reveals how Legionella uses molecular mimicry to manipulate the host ubiquitination pathway and proliferate intracellularly.
-Structural Mimicry by a Bacterial F Box Effector Hijacks the Host Ubiquitin-Proteasome System.,Wong K, Perpich JD, Kozlov G, Cygler M, Abu Kwaik Y, Gehring K Structure. 2017 Feb 7;25(2):376-383. doi: 10.1016/j.str.2016.12.015. Epub 2017, Jan 19. PMID:28111017<ref>PMID:28111017</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 5k34" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Ankyrin 3D structures|Ankyrin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 33152]]
 [[Category: Large Structures]]
-[[Category: Structural genomic]]
+[[Category: Legionella pneumophila]]
-[[Category: Gehring, K]]
+[[Category: Gehring K]]
-[[Category: Kozlov, G]]
+[[Category: Kozlov G]]
-[[Category: Wong, K]]
+[[Category: Wong K]]
-[[Category: Ankyrin domain]]
-[[Category: Bacterial effector]]
-[[Category: Bsgi]]
-[[Category: Protein binding]]
-[[Category: Protein-protein interaction]]

5k34

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Structure of the ankyrin domain of AnkB from Legionella Pneumophila

Structural highlights

Function

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