6ks5

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:44, 27 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='6ks5' size='340' side='right'caption='[[6ks5]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='6ks5' size='340' side='right'caption='[[6ks5]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6ks5]] is a 2 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=6KS5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KS5 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6ks5]] is a 2 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=6KS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KS5 FirstGlance]. <br>
-
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C3927_07335 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=446 ATCC 33152])</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]] 2.8&#8491;</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=6ks5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ks5 OCA], [http://pdbe.org/6ks5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ks5 RCSB], [http://www.ebi.ac.uk/pdbsum/6ks5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ks5 ProSAT]</span></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=6ks5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ks5 OCA], [https://pdbe.org/6ks5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ks5 RCSB], [https://www.ebi.ac.uk/pdbsum/6ks5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ks5 ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/Q5ZV21_LEGPH Q5ZV21_LEGPH]
-
Legionella pneumophila is the causative agent of the lung malady Legionnaires' disease, it modulates host function to create a niche termed the Legionella-containing vacuole (LCV) that permits intracellular L. pneumophila replication. One important aspect of such modulation is the co-option of the host ubiquitin network with a panel of effector proteins. Here, using recombinantly expressed and purified proteins, analytic ultracentrifugation, structural analysis, and computational modeling, along with deubiquitinase (DUB), and bacterial infection assays, we found that the bacterial defective in organelle trafficking/intracellular multiplication effector Ceg23 is a member of the ovarian tumor (OTU) DUB family. We found that Ceg23 displays high specificity toward Lys-63-linked polyubiquitin chains and is localized on the LCV, where it removes ubiquitin moieties from proteins ubiquitinated by the Lys-63-chain type. Analysis of the crystal structure of a Ceg23 variant lacking two putative transmembrane domains at 2.80 A resolution revealed that despite very limited homology to established members of the OTU family at the primary sequence level, Ceg23 harbors a catalytic motif resembling those associated with typical OTU-type DUBs. ceg23 deletion increased the association of Lys-63-linked polyubiquitin with the bacterial phagosome, indicating that Ceg23 regulates Lys-63-linked ubiquitin signaling on the LCV. In summary, our findings indicate that Ceg23 contributes to the regulation of the association of Lys-63 type polyubiquitin with the Legionella phagosome. Future identification of host substrates targeted by Ceg23 could clarify the roles of these polyubiquitin chains in the intracellular life cycle of L. pneumophila and Ceg23's role in bacterial virulence.
+
-
 
+
-
The bacterial deubiquitinase Ceg23 regulates the association of Lys-63-linked polyubiquitin molecules on the Legionella phagosome.,Ma K, Zhen X, Zhou B, Gan N, Cao Y, Fan C, Ouyang S, Luo ZQ, Qiu J J Biol Chem. 2020 Feb 7;295(6):1646-1657. doi: 10.1074/jbc.RA119.011758. Epub, 2020 Jan 6. PMID:31907282<ref>PMID:31907282</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 6ks5" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Atcc 33152]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Ouyang, S Y]]
+
[[Category: Legionella pneumophila]]
-
[[Category: Qiu, J Z]]
+
[[Category: Ouyang SY]]
-
[[Category: Enzyme]]
+
[[Category: Qiu JZ]]
-
[[Category: Hydrolase]]
+

Current revision

Crystal structure of Legionella pneumophila deubiquitinase Ceg23

PDB ID 6ks5

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools