Crystal structures of Cif from bacterial pathogens Photorhabdus luminescens and Burkholderia pseudomallei.
A pre-requisite for bacterial pathogenesis is the successful interaction of a pathogen with a host. One mechanism used by a broad range of Gram negative bacterial pathogens is to deliver effector proteins directly into host cells through a dedicated type III secretion system where they modulate host...
Saved in:
| Main Authors: | , , , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2009-01-01
|
| Series: | PLoS ONE |
| Online Access: | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0005582&type=printable |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1850240400536633344 |
|---|---|
| author | Allister Crow Paul R Race Grégory Jubelin Carolina Varela Chavez Jean-Michel Escoubas Eric Oswald Mark J Banfield |
| author_facet | Allister Crow Paul R Race Grégory Jubelin Carolina Varela Chavez Jean-Michel Escoubas Eric Oswald Mark J Banfield |
| author_sort | Allister Crow |
| collection | DOAJ |
| description | A pre-requisite for bacterial pathogenesis is the successful interaction of a pathogen with a host. One mechanism used by a broad range of Gram negative bacterial pathogens is to deliver effector proteins directly into host cells through a dedicated type III secretion system where they modulate host cell function. The cycle inhibiting factor (Cif) family of effector proteins, identified in a growing number of pathogens that harbour functional type III secretion systems and have a wide host range, arrest the eukaryotic cell cycle. Here, the crystal structures of Cifs from the insect pathogen/nematode symbiont Photorhabdus luminescens (a gamma-proteobacterium) and human pathogen Burkholderia pseudomallei (a beta-proteobacterium) are presented. Both of these proteins adopt an overall fold similar to the papain sub-family of cysteine proteases, as originally identified in the structure of a truncated form of Cif from Enteropathogenic E. coli (EPEC), despite sharing only limited sequence identity. The structure of an N-terminal region, referred to here as the 'tail-domain' (absent in the EPEC Cif structure), suggests a surface likely to be involved in host-cell substrate recognition. The conformation of the Cys-His-Gln catalytic triad is retained, and the essential cysteine is exposed to solvent and addressable by small molecule reagents. These structures and biochemical work contribute to the rapidly expanding literature on Cifs, and direct further studies to better understand the molecular details of the activity of these proteins. |
| format | Article |
| id | doaj-art-9eb2182beea542148ede3bfbef2b1d26 |
| institution | OA Journals |
| issn | 1932-6203 |
| language | English |
| publishDate | 2009-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj-art-9eb2182beea542148ede3bfbef2b1d262025-08-20T02:00:52ZengPublic Library of Science (PLoS)PLoS ONE1932-62032009-01-0145e558210.1371/journal.pone.0005582Crystal structures of Cif from bacterial pathogens Photorhabdus luminescens and Burkholderia pseudomallei.Allister CrowPaul R RaceGrégory JubelinCarolina Varela ChavezJean-Michel EscoubasEric OswaldMark J BanfieldA pre-requisite for bacterial pathogenesis is the successful interaction of a pathogen with a host. One mechanism used by a broad range of Gram negative bacterial pathogens is to deliver effector proteins directly into host cells through a dedicated type III secretion system where they modulate host cell function. The cycle inhibiting factor (Cif) family of effector proteins, identified in a growing number of pathogens that harbour functional type III secretion systems and have a wide host range, arrest the eukaryotic cell cycle. Here, the crystal structures of Cifs from the insect pathogen/nematode symbiont Photorhabdus luminescens (a gamma-proteobacterium) and human pathogen Burkholderia pseudomallei (a beta-proteobacterium) are presented. Both of these proteins adopt an overall fold similar to the papain sub-family of cysteine proteases, as originally identified in the structure of a truncated form of Cif from Enteropathogenic E. coli (EPEC), despite sharing only limited sequence identity. The structure of an N-terminal region, referred to here as the 'tail-domain' (absent in the EPEC Cif structure), suggests a surface likely to be involved in host-cell substrate recognition. The conformation of the Cys-His-Gln catalytic triad is retained, and the essential cysteine is exposed to solvent and addressable by small molecule reagents. These structures and biochemical work contribute to the rapidly expanding literature on Cifs, and direct further studies to better understand the molecular details of the activity of these proteins.https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0005582&type=printable |
| spellingShingle | Allister Crow Paul R Race Grégory Jubelin Carolina Varela Chavez Jean-Michel Escoubas Eric Oswald Mark J Banfield Crystal structures of Cif from bacterial pathogens Photorhabdus luminescens and Burkholderia pseudomallei. PLoS ONE |
| title | Crystal structures of Cif from bacterial pathogens Photorhabdus luminescens and Burkholderia pseudomallei. |
| title_full | Crystal structures of Cif from bacterial pathogens Photorhabdus luminescens and Burkholderia pseudomallei. |
| title_fullStr | Crystal structures of Cif from bacterial pathogens Photorhabdus luminescens and Burkholderia pseudomallei. |
| title_full_unstemmed | Crystal structures of Cif from bacterial pathogens Photorhabdus luminescens and Burkholderia pseudomallei. |
| title_short | Crystal structures of Cif from bacterial pathogens Photorhabdus luminescens and Burkholderia pseudomallei. |
| title_sort | crystal structures of cif from bacterial pathogens photorhabdus luminescens and burkholderia pseudomallei |
| url | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0005582&type=printable |
| work_keys_str_mv | AT allistercrow crystalstructuresofciffrombacterialpathogensphotorhabdusluminescensandburkholderiapseudomallei AT paulrrace crystalstructuresofciffrombacterialpathogensphotorhabdusluminescensandburkholderiapseudomallei AT gregoryjubelin crystalstructuresofciffrombacterialpathogensphotorhabdusluminescensandburkholderiapseudomallei AT carolinavarelachavez crystalstructuresofciffrombacterialpathogensphotorhabdusluminescensandburkholderiapseudomallei AT jeanmichelescoubas crystalstructuresofciffrombacterialpathogensphotorhabdusluminescensandburkholderiapseudomallei AT ericoswald crystalstructuresofciffrombacterialpathogensphotorhabdusluminescensandburkholderiapseudomallei AT markjbanfield crystalstructuresofciffrombacterialpathogensphotorhabdusluminescensandburkholderiapseudomallei |