5jui

From Proteopedia

(Difference between revisions)

Current revision

domain-swapped dimer of the the KRT10-binding region (BR) of PsrP

Structural highlights

5jui is a 3 chain structure with sequence from Streptococcus pneumoniae TIGR4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PSRP_STRPN Protein that allows bacteria to adhere to mammalian host cells. Required for full virulence in mouse infection models when infected intranasally (PubMed:16861665). Required for adhesion to host cells in vitro and for persistence in the lower respiratory tract (PubMed:18507531). Binds host keratin 10 (KRT10) on lung cells which mediates adhesion via the C-terminus of the basic region (BR, residues 273-341); glycosylation of either protein is not required for the interaction (PubMed:19627498). A region in the N-terminus (residues 122-166) self aggregates, contributing to mature biofilm formation (PubMed:20714350). The basic region (BR, residues 187-385) also self aggregates; the BR binds DNA which enhances self aggregation (PubMed:27582320).^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

The major human pathogen Streptococcus pneumoniae is a leading cause of disease and death worldwide. Pneumococcal biofilm formation within the nasopharynx leads to long-term colonization and persistence within the host. We have previously demonstrated that the capsular surface-associated pneumococcal serine rich repeat protein (PsrP), key factor for biofilm formation, binds to keratin-10 (KRT10) through its microbial surface component recognizing adhesive matrix molecule (MSCRAMM)-related globular binding region domain (BR187-385). Here, we show that BR187-385 also binds to DNA, as demonstrated by electrophoretic mobility shift assays and size exclusion chromatography. Further, heterologous expression of BR187-378 or the longer BR120-378 construct on the surface of a Gram-positive model host bacterium resulted in the formation of cellular aggregates that was significantly enhanced in the presence of DNA. Crystal structure analyses revealed the formation of BR187-385 homo-dimers via an intermolecular beta-sheet, resulting in a positively charged concave surface, shaped to accommodate the acidic helical DNA structure. Furthermore, small angle X-ray scattering and circular dichroism studies indicate that the aggregate-enhancing N-terminal region of BR120-166 adopts an extended, non-globular structure. Altogether, our results suggest that PsrP adheres to extracellular DNA in the biofilm matrix and thus promotes pneumococcal biofilm formation.

The BR domain of PsrP interacts with extracellular DNA to promote bacterial aggregation; structural insights into pneumococcal biofilm formation.,Schulte T, Mikaelsson C, Beaussart A, Kikhney A, Deshmukh M, Wolniak S, Pathak A, Ebel C, Lofling J, Fogolari F, Henriques-Normark B, Dufrene YF, Svergun D, Nygren PA, Achour A Sci Rep. 2016 Sep 1;6:32371. doi: 10.1038/srep32371. PMID:27582320^[6]

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

References

↑ Obert C, Sublett J, Kaushal D, Hinojosa E, Barton T, Tuomanen EI, Orihuela CJ. Identification of a Candidate Streptococcus pneumoniae core genome and regions of diversity correlated with invasive pneumococcal disease. Infect Immun. 2006 Aug;74(8):4766-77. PMID:16861665 doi:10.1128/IAI.00316-06
↑ Rose L, Shivshankar P, Hinojosa E, Rodriguez A, Sanchez CJ, Orihuela CJ. Antibodies against PsrP, a novel Streptococcus pneumoniae adhesin, block adhesion and protect mice against pneumococcal challenge. J Infect Dis. 2008 Aug 1;198(3):375-83. PMID:18507531 doi:10.1086/589775
↑ Shivshankar P, Sanchez C, Rose LF, Orihuela CJ. The Streptococcus pneumoniae adhesin PsrP binds to Keratin 10 on lung cells. Mol Microbiol. 2009 Aug;73(4):663-79. PMID:19627498 doi:10.1111/j.1365-2958.2009.06796.x
↑ Sanchez CJ, Shivshankar P, Stol K, Trakhtenbroit S, Sullam PM, Sauer K, Hermans PW, Orihuela CJ. The pneumococcal serine-rich repeat protein is an intra-species bacterial adhesin that promotes bacterial aggregation in vivo and in biofilms. PLoS Pathog. 2010 Aug 12;6(8):e1001044. PMID:20714350 doi:10.1371/journal.ppat.1001044
↑ Schulte T, Mikaelsson C, Beaussart A, Kikhney A, Deshmukh M, Wolniak S, Pathak A, Ebel C, Lofling J, Fogolari F, Henriques-Normark B, Dufrene YF, Svergun D, Nygren PA, Achour A. The BR domain of PsrP interacts with extracellular DNA to promote bacterial aggregation; structural insights into pneumococcal biofilm formation. Sci Rep. 2016 Sep 1;6:32371. doi: 10.1038/srep32371. PMID:27582320 doi:http://dx.doi.org/10.1038/srep32371
↑ Schulte T, Mikaelsson C, Beaussart A, Kikhney A, Deshmukh M, Wolniak S, Pathak A, Ebel C, Lofling J, Fogolari F, Henriques-Normark B, Dufrene YF, Svergun D, Nygren PA, Achour A. The BR domain of PsrP interacts with extracellular DNA to promote bacterial aggregation; structural insights into pneumococcal biofilm formation. Sci Rep. 2016 Sep 1;6:32371. doi: 10.1038/srep32371. PMID:27582320 doi:http://dx.doi.org/10.1038/srep32371

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5jui"

Categories: Large Structures | Streptococcus pneumoniae TIGR4 | Achour A | Mikaelsson C | Schulte T

@@ Line 3: / Line 3: @@
 <StructureSection load='5jui' size='340' side='right'caption='[[5jui]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5jui]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JUI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5JUI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5jui]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_TIGR4 Streptococcus pneumoniae TIGR4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JUI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JUI FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zgh|3zgh]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=5jui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jui OCA], [http://pdbe.org/5jui PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jui RCSB], [http://www.ebi.ac.uk/pdbsum/5jui PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jui ProSAT]</span></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=5jui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jui OCA], [https://pdbe.org/5jui PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jui RCSB], [https://www.ebi.ac.uk/pdbsum/5jui PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jui ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/PSRP_STRPN PSRP_STRPN] Protein that allows bacteria to adhere to mammalian host cells. Required for full virulence in mouse infection models when infected intranasally (PubMed:16861665). Required for adhesion to host cells in vitro and for persistence in the lower respiratory tract (PubMed:18507531). Binds host keratin 10 (KRT10) on lung cells which mediates adhesion via the C-terminus of the basic region (BR, residues 273-341); glycosylation of either protein is not required for the interaction (PubMed:19627498). A region in the N-terminus (residues 122-166) self aggregates, contributing to mature biofilm formation (PubMed:20714350). The basic region (BR, residues 187-385) also self aggregates; the BR binds DNA which enhances self aggregation (PubMed:27582320).<ref>PMID:16861665</ref> <ref>PMID:18507531</ref> <ref>PMID:19627498</ref> <ref>PMID:20714350</ref> <ref>PMID:27582320</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 24: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Achour, A]]
+[[Category: Streptococcus pneumoniae TIGR4]]
-[[Category: Mikaelsson, C]]
+[[Category: Achour A]]
-[[Category: Schulte, T]]
+[[Category: Mikaelsson C]]
-[[Category: Bacterial aggregation]]
+[[Category: Schulte T]]
-[[Category: Biofilm formation]]
-[[Category: Dna]]
-[[Category: Oligomerisation]]
-[[Category: Pneumococcal serine rich repeat protein]]
-[[Category: Streptococcus pneumoniae]]
-[[Category: Structural protein]]

5jui

From Proteopedia

Current revision

domain-swapped dimer of the the KRT10-binding region (BR) of PsrP

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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