View source for 4bvu


==Structure of Shigella effector OspG in complex with host UbcH5c- Ubiquitin conjugate==
<StructureSection load='4bvu' size='340' side='right'caption='[[4bvu]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bvu]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BVU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BVU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</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=4bvu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bvu OCA], [https://pdbe.org/4bvu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bvu RCSB], [https://www.ebi.ac.uk/pdbsum/4bvu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bvu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OSPG_SHIFL OSPG_SHIFL] Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is a kinase that is involved in down-regulation of the host innate response induced by invasive bacteria. Prevents or at least delays host phospho-NF-kappa-B inhibitor alpha (NFKBIA) degradation. Does not phosphorylate E2 enzymes.<ref>PMID:16162672</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pathogenic bacteria introduce effector proteins directly into the cytosol of eukaryotic cells to promote invasion and colonization. OspG, a Shigella spp. effector kinase, plays a role in this process by helping to suppress the host inflammatory response. OspG has been reported to bind host E2 ubiquitin-conjugating enzymes activated with ubiquitin (E2~Ub), a key enzyme complex in ubiquitin transfer pathways. A co-crystal structure of the OspG/UbcH5c~Ub complex reveals that complex formation has important ramifications for the activity of both OspG and the UbcH5c~Ub conjugate. OspG is a minimal kinase domain containing only essential elements required for catalysis. UbcH5c~Ub binding stabilizes an active conformation of the kinase, greatly enhancing OspG kinase activity. In contrast, interaction with OspG stabilizes an extended, less reactive form of UbcH5c~Ub. Recognizing conserved E2 features, OspG can interact with at least ten distinct human E2s~Ub. Mouse oral infection studies indicate that E2~Ub conjugates act as novel regulators of OspG effector kinase function in eukaryotic host cells.

E2~Ub conjugates regulate the kinase activity of Shigella effector OspG during pathogenesis.,Pruneda JN, Smith FD, Daurie A, Swaney DL, Villen J, Scott JD, Stadnyk AW, Le Trong I, Stenkamp RE, Klevit RE, Rohde JR, Brzovic PS EMBO J. 2014 Jan 20. PMID:24446487<ref>PMID:24446487</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bvu" style="background-color:#fffaf0;"></div>

==See Also==
*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Shigella flexneri]]
[[Category: Brzovic PS]]
[[Category: Klevit RE]]
[[Category: LeTrong I]]
[[Category: Pruneda JN]]
[[Category: Stenkamp RE]]