3g06

<table><tr><td colspan='2'>[[3g06]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G06 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3G06 FirstGlance]. <br>

</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin--protein_ligase Ubiquitin--protein ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.19 6.3.2.19] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3g06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g06 OCA], [http://pdbe.org/3g06 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g06 RCSB], [http://www.ebi.ac.uk/pdbsum/3g06 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3g06 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/SSPH2_SALT1 SSPH2_SALT1]] Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Contributes to virulence in calves.<ref>PMID:10564523</ref> <ref>PMID:19273841</ref>

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== Publication Abstract from PubMed ==

Processes as diverse as receptor binding and signaling, cytoskeletal dynamics, and programmed cell death are manipulated by mimics of host proteins encoded by pathogenic bacteria. We show here that the Salmonella virulence factor SspH2 belongs to a growing class of bacterial effector proteins that harness and subvert the eukaryotic ubiquitination pathway. This virulence protein possesses ubiquitination activity that depends on a conserved cysteine residue. A crystal structure of SspH2 reveals a canonical leucine-rich repeat (LRR) domain that interacts with a unique E3 ligase [which we have termed NEL for Novel E3 Ligase] C-terminal fold unrelated to previously observed HECT or RING-finger E3 ligases. Moreover, the LRR domain sequesters the catalytic cysteine residue contained in the NEL domain, and we suggest a mechanism for activation of the ligase requiring a substantial conformational change to release the catalytic domain for function. We also show that the N-terminal domain targets SspH2 to the apical plasma membrane of polarized epithelial cells and propose a model whereby binding of the LRR to proteins at the target site releases the ligase domain for site-specific function.

A family of Salmonella virulence factors functions as a distinct class of autoregulated E3 ubiquitin ligases.,Quezada CM, Hicks SW, Galan JE, Stebbins CE Proc Natl Acad Sci U S A. 2009 Mar 24;106(12):4864-9. Epub 2009 Mar 9. PMID:19273841<ref>PMID:19273841</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Ubiquitin--protein ligase]]

[[Category: Quezada, C M]]

[[Category: Stebbins, C E]]

[[Category: Type three effector]]