3zgi

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the KRT10-binding region domain of the pneumococcal serine rich repeat protein PsrP

Structural highlights

3zgi 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 2.25Å
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

Streptococcus pneumoniae is a major human pathogen, and a leading cause of disease and death worldwide. Pneumococcal invasive disease is triggered by initial asymptomatic colonization of the human upper respiratory tract. The pneumococcal serine-rich repeat protein (PsrP) is a lung-specific virulence factor whose functional binding region (BR) binds to keratin-10 (KRT10) and promotes pneumococcal biofilm formation through self-oligomerization. We present the crystal structure of the KRT10-binding domain of PsrP (BR187-385) determined to 2.0 A resolution. BR187-385 adopts a novel variant of the DEv-IgG fold, typical for microbial surface components recognizing adhesive matrix molecules adhesins, despite very low sequence identity. An extended beta-sheet on one side of the compressed, two-sided barrel presents a basic groove that possibly binds to the acidic helical rod domain of KRT10. Our study also demonstrates the importance of the other side of the barrel, formed by extensive well-ordered loops and stabilized by short beta-strands, for interaction with KRT10.

The basic keratin 10-binding domain of the virulence-associated pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold.,Schulte T, Lofling J, Mikaelsson C, Kikhney A, Hentrich K, Diamante A, Ebel C, Normark S, Svergun D, Henriques-Normark B, Achour A Open Biol. 2014 Jan 15;4(1):130090. doi: 10.1098/rsob.130090. PMID:24430336^[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, Lofling J, Mikaelsson C, Kikhney A, Hentrich K, Diamante A, Ebel C, Normark S, Svergun D, Henriques-Normark B, Achour A. The basic keratin 10-binding domain of the virulence-associated pneumococcal serine-rich protein PsrP adopts a novel MSCRAMM fold. Open Biol. 2014 Jan 15;4(1):130090. doi: 10.1098/rsob.130090. PMID:24430336 doi:http://dx.doi.org/10.1098/rsob.130090

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/3zgi"

@@ Line 3: / Line 3: @@
 <StructureSection load='3zgi' size='340' side='right'caption='[[3zgi]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3zgi]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Strpn Strpn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZGI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZGI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3zgi]] 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=3ZGI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZGI FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.25&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zgh|3zgh]]</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=3zgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zgi OCA], [https://pdbe.org/3zgi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zgi RCSB], [https://www.ebi.ac.uk/pdbsum/3zgi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zgi ProSAT]</span></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=3zgi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zgi OCA], [http://pdbe.org/3zgi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zgi RCSB], [http://www.ebi.ac.uk/pdbsum/3zgi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zgi 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 23: / Line 24: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Strpn]]
+[[Category: Streptococcus pneumoniae TIGR4]]
-[[Category: Achour, A]]
+[[Category: Achour A]]
-[[Category: Diamante, A]]
+[[Category: Diamante A]]
-[[Category: Ebel, C]]
+[[Category: Ebel C]]
-[[Category: Henriques-Normark, B]]
+[[Category: Henriques-Normark B]]
-[[Category: Hentrich, K]]
+[[Category: Hentrich K]]
-[[Category: Kikhney, A]]
+[[Category: Kikhney A]]
-[[Category: Loefling, J]]
+[[Category: Loefling J]]
-[[Category: Mikaelsson, C]]
+[[Category: Mikaelsson C]]
-[[Category: Normark, S]]
+[[Category: Normark S]]
-[[Category: Schulte, T]]
+[[Category: Schulte T]]
-[[Category: Svergun, D]]
+[[Category: Svergun D]]
-[[Category: Adhesin]]
-[[Category: Keratin-10]]
-[[Category: Srrp]]
-[[Category: Structural protein]]

3zgi

From Proteopedia

Current revision

Crystal structure of the KRT10-binding region domain of the pneumococcal serine rich repeat protein PsrP

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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