3l3p

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Template:STRUCTURE 3l3p

Contents 1 Crystal structure of the C-terminal domain of Shigella type III effector IpaH9.8, with a novel domain swap 2 Function 3 About this Structure 4 Reference

Crystal structure of the C-terminal domain of Shigella type III effector IpaH9.8, with a novel domain swap

Template:ABSTRACT PUBMED 20831869

Function

[IPA9_SHIFL] 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 and modulates the acute inflammatory responses, thus facilitating bacterial colonization within the host cell. Interacts with IKBKG (NEMO) and TNIP1 (ABIN-1), an ubiquitin-binding adapter protein, which results in TNIP1-dependent 'Lys-27'-linked polyubiquitination of IKBKG. Consequently, polyubiquitinated IKBKG undergoes proteasome-dependent degradation, which perturbs NF-kappa-B activation during bacterial infection. Uses UBE2D2 (UBCH5B) as an E2 ubiquitin-conjugating enzyme.^{[1] [2] [3]}

About this Structure

3l3p is a 1 chain structure with sequence from Shigella flexneri. Full crystallographic information is available from OCA.

Reference

• Seyedarabi A, Sullivan JA, Sasakawa C, Pickersgill RW. A disulfide driven domain swap switches off the activity of Shigella IpaH9.8 E3 ligase. FEBS Lett. 2010 Oct 8;584(19):4163-8. Epub 2010 Sep 8. PMID:20831869 doi:10.1016/j.febslet.2010.09.006

1. ↑ Okuda J, Toyotome T, Kataoka N, Ohno M, Abe H, Shimura Y, Seyedarabi A, Pickersgill R, Sasakawa C. Shigella effector IpaH9.8 binds to a splicing factor U2AF(35) to modulate host immune responses. Biochem Biophys Res Commun. 2005 Jul 29;333(2):531-9. PMID:15950937 doi:10.1016/j.bbrc.2005.05.145
2. ↑ Rohde JR, Breitkreutz A, Chenal A, Sansonetti PJ, Parsot C. Type III secretion effectors of the IpaH family are E3 ubiquitin ligases. Cell Host Microbe. 2007 Mar 15;1(1):77-83. PMID:18005683 doi:10.1016/j.chom.2007.02.002
3. ↑ Ashida H, Kim M, Schmidt-Supprian M, Ma A, Ogawa M, Sasakawa C. A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response. Nat Cell Biol. 2010 Jan;12(1):66-73; sup pp 1-9. doi: 10.1038/ncb2006. Epub 2009 , Dec 13. PMID:20010814 doi:10.1038/ncb2006