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1xkp

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Revision as of 10:05, 6 January 2021

Crystal structure of the virulence factor YopN in complex with its heterodimeric chaperone SycN-YscB

Structural highlights

1xkp is a 3 chain structure with sequence from "bacillus_pestis"_(lehmann_and_neumann_1896)_migula_1900 "bacillus pestis" (lehmann and neumann 1896) migula 1900. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:	,
Gene:	yopN ("Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900), sycN ("Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900), yscB ("Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[YSCB_YERPE] Functions as a specific chaperone for YopN. It could facilitate the secretion and the subsequent translocation of YopN.^[1] ^[2] ^[3] [SYCN_YERPE] Functions as a specific chaperone for YopN. It could facilitate the secretion and the subsequent translocation of YopN.^[4] ^[5]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Yersinia pestis, the causative agent of plague, utilizes a type III secretion system (T3SS) to inject effector proteins directly into the cytosol of mammalian cells where they interfere with signal transduction pathways that regulate actin cytoskeleton dynamics and inflammation, thereby enabling the bacterium to avoid engulfment and destruction by macrophages. Type III secretion normally does not occur in the absence of close contact with eukaryotic cells. Negative regulation is mediated in part by a multiprotein complex that has been proposed to act as a physical impediment to type III secretion by blocking the entrance to the secretion apparatus prior to contact with mammalian cells. This complex is composed of YopN, its heterodimeric secretion chaperone SycN-YscB, and TyeA. Here, we report two crystal structures of YopN in complex with its heterodimeric secretion chaperone SycN-YscB and the co-regulatory protein TyeA, respectively. By merging these two overlapping structures, it was possible to construct a credible theoretical model of the YopN-SycN-YscB-TyeA complex. The modeled assembly features the secretion signaling elements of YopN at one end of an elongated structure and the secretion regulating TyeA binding site at the other. A patch of highly conserved residues on the surface of the C-terminal alpha-helix of TyeA may mediate its interaction with structural components of the secretion apparatus. Conserved arginine residues that reside inside a prominent cavity at the dimer interface of SycN-YscB were mutated in order to investigate whether they play a role in targeting the YopN-chaperone complex to the type III secretion apparatus. One of the mutants exhibited a phenotype that is consistent with this hypothesis.

Three-dimensional structure of a macromolecular assembly that regulates type III secretion in Yersinia pestis.,Schubot FD, Jackson MW, Penrose KJ, Cherry S, Tropea JE, Plano GV, Waugh DS J Mol Biol. 2005 Mar 4;346(4):1147-61. Epub 2005 Jan 20. PMID:15701523^[6]

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

References

↑ Jackson MW, Day JB, Plano GV. YscB of Yersinia pestis functions as a specific chaperone for YopN. J Bacteriol. 1998 Sep;180(18):4912-21. PMID:9733695
↑ Day JB, Plano GV. A complex composed of SycN and YscB functions as a specific chaperone for YopN in Yersinia pestis. Mol Microbiol. 1998 Nov;30(4):777-88. PMID:10094626
↑ Day JB, Ferracci F, Plano GV. Translocation of YopE and YopN into eukaryotic cells by Yersinia pestis yopN, tyeA, sycN, yscB and lcrG deletion mutants measured using a phosphorylatable peptide tag and phosphospecific antibodies. Mol Microbiol. 2003 Feb;47(3):807-23. PMID:12535078
↑ Day JB, Plano GV. A complex composed of SycN and YscB functions as a specific chaperone for YopN in Yersinia pestis. Mol Microbiol. 1998 Nov;30(4):777-88. PMID:10094626
↑ Day JB, Ferracci F, Plano GV. Translocation of YopE and YopN into eukaryotic cells by Yersinia pestis yopN, tyeA, sycN, yscB and lcrG deletion mutants measured using a phosphorylatable peptide tag and phosphospecific antibodies. Mol Microbiol. 2003 Feb;47(3):807-23. PMID:12535078
↑ Schubot FD, Jackson MW, Penrose KJ, Cherry S, Tropea JE, Plano GV, Waugh DS. Three-dimensional structure of a macromolecular assembly that regulates type III secretion in Yersinia pestis. J Mol Biol. 2005 Mar 4;346(4):1147-61. Epub 2005 Jan 20. PMID:15701523 doi:10.1016/j.jmb.2004.12.036

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Crystal structure of the virulence factor YopN in complex with its heterodimeric chaperone SycN-YscB==
-<StructureSection load='1xkp' size='340' side='right' caption='[[1xkp]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+<StructureSection load='1xkp' size='340' side='right'caption='[[1xkp]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1xkp]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pestis"_(lehmann_and_neumann_1896)_migula_1900 "bacillus pestis" (lehmann and neumann 1896) migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XKP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XKP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1xkp]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pestis"_(lehmann_and_neumann_1896)_migula_1900 "bacillus pestis" (lehmann and neumann 1896) migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XKP OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XKP FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMG:N,N-DIMETHYLGLYCINE'>DMG</scene>, <scene name='pdbligand=MLY:N-DIMETHYL-LYSINE'>MLY</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yopN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=632 "Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900]), sycN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=632 "Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900]), yscB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=632 "Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900])</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=1xkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xkp OCA], [http://pdbe.org/1xkp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xkp RCSB], [http://www.ebi.ac.uk/pdbsum/1xkp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xkp ProSAT]</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=1xkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xkp OCA], [http://pdbe.org/1xkp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xkp RCSB], [http://www.ebi.ac.uk/pdbsum/1xkp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xkp ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 33: / Line 33: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Cherry, S]]
 [[Category: Jackson, M W]]

1xkp

From Proteopedia

Revision as of 10:05, 6 January 2021

Crystal structure of the virulence factor YopN in complex with its heterodimeric chaperone SycN-YscB

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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