1jyo

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Revision as of 08:44, 21 April 2021

Structure of the Salmonella Virulence Effector SptP in Complex with its Secretion Chaperone SicP

Structural highlights

1jyo is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SICP_SALTY] Molecular chaperone required for sptP stabilization and secretion. [SPTP_SALTY] Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein includes tyrosine phosphatase and GTPase activating protein (GAP) activities. After bacterial internalization, GAP mediates the reversal of the cytoskeletal changes induced by SopE. This function is independent of its tyrosine phosphatase activity, which remains unclear.^[1] ^[2] ^[3]

Publication Abstract from PubMed

Many bacterial pathogens use a type III protein secretion system to deliver virulence effector proteins directly into the host cell cytosol, where they modulate cellular processes. A requirement for the effective translocation of several such effector proteins is the binding of specific cytosolic chaperones, which typically interact with discrete domains in the virulence factors. We report here the crystal structure at 1.9 A resolution of the chaperone-binding domain of the Salmonella effector protein SptP with its cognate chaperone SicP. The structure reveals that this domain is maintained in an extended, unfolded conformation that is wound around three successive chaperone molecules. Short segments from two different SptP molecules are juxtaposed by the chaperones, where they dimerize across a hydrophobic interface. These results imply that the chaperones associated with the type III secretion system maintain their substrates in a secretion-competent state that is capable of engaging the secretion machinery to travel through the type III apparatus in an unfolded or partially folded manner.

Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion.,Stebbins CE, Galan JE Nature. 2001 Nov 1;414(6859):77-81. PMID:11689946^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Kaniga K, Uralil J, Bliska JB, Galan JE. A secreted protein tyrosine phosphatase with modular effector domains in the bacterial pathogen Salmonella typhimurium. Mol Microbiol. 1996 Aug;21(3):633-41. PMID:8866485
↑ Fu Y, Galan JE. A salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion. Nature. 1999 Sep 16;401(6750):293-7. PMID:10499590 doi:http://dx.doi.org/10.1038/45829
↑ Stebbins CE, Galan JE. Modulation of host signaling by a bacterial mimic: structure of the Salmonella effector SptP bound to Rac1. Mol Cell. 2000 Dec;6(6):1449-60. PMID:11163217
↑ Stebbins CE, Galan JE. Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion. Nature. 2001 Nov 1;414(6859):77-81. PMID:11689946 doi:10.1038/35102073

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jyo"

@@ Line 3: / Line 3: @@
 <StructureSection load='1jyo' size='340' side='right'caption='[[1jyo]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1jyo]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JYO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JYO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1jyo]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JYO FirstGlance]. <br>
-</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=1jyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jyo OCA], [http://pdbe.org/1jyo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jyo RCSB], [http://www.ebi.ac.uk/pdbsum/1jyo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jyo ProSAT]</span></td></tr>
+</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=1jyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jyo OCA], [https://pdbe.org/1jyo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jyo RCSB], [https://www.ebi.ac.uk/pdbsum/1jyo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jyo ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SICP_SALTY SICP_SALTY]] Molecular chaperone required for sptP stabilization and secretion. [[http://www.uniprot.org/uniprot/SPTP_SALTY SPTP_SALTY]] Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein includes tyrosine phosphatase and GTPase activating protein (GAP) activities. After bacterial internalization, GAP mediates the reversal of the cytoskeletal changes induced by SopE. This function is independent of its tyrosine phosphatase activity, which remains unclear.<ref>PMID:8866485</ref> <ref>PMID:10499590</ref> <ref>PMID:11163217</ref>
+[[https://www.uniprot.org/uniprot/SICP_SALTY SICP_SALTY]] Molecular chaperone required for sptP stabilization and secretion. [[https://www.uniprot.org/uniprot/SPTP_SALTY SPTP_SALTY]] Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein includes tyrosine phosphatase and GTPase activating protein (GAP) activities. After bacterial internalization, GAP mediates the reversal of the cytoskeletal changes induced by SopE. This function is independent of its tyrosine phosphatase activity, which remains unclear.<ref>PMID:8866485</ref> <ref>PMID:10499590</ref> <ref>PMID:11163217</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 19: @@
 ==See Also==
-*[[Tyrosine phosphatase|Tyrosine phosphatase]]
+*[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]]
 == References ==
 <references/>

1jyo

From Proteopedia

Revision as of 08:44, 21 April 2021

Structure of the Salmonella Virulence Effector SptP in Complex with its Secretion Chaperone SicP

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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