3zgi

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(New page: '''Unreleased structure''' The entry 3zgi is ON HOLD Authors: Schulte, T., Loefling, J., Mikaelsson, C., Kikhney, A., Hentrich, K., Diamante, A., Ebel, C., Normark, S., Svergun, D., Hen...)
Current revision (06:19, 17 October 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 3zgi is ON HOLD
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==Crystal structure of the KRT10-binding region domain of the pneumococcal serine rich repeat protein PsrP==
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<StructureSection load='3zgi' size='340' side='right'caption='[[3zgi]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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<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>
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<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>
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</table>
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== Function ==
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Schulte, T., Loefling, J., Mikaelsson, C., Kikhney, A., Hentrich, K., Diamante, A., Ebel, C., Normark, S., Svergun, D., Henriques-Normark, B., Achour, A.
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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<ref>PMID:24430336</ref>
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Description: Crystal structure of the KRT10-binding region domain of the pneumococcal serine rich repeat protein PsrP
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3zgi" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Streptococcus pneumoniae TIGR4]]
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[[Category: Achour A]]
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[[Category: Diamante A]]
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[[Category: Ebel C]]
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[[Category: Henriques-Normark B]]
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[[Category: Hentrich K]]
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[[Category: Kikhney A]]
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[[Category: Loefling J]]
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[[Category: Mikaelsson C]]
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[[Category: Normark S]]
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[[Category: Schulte T]]
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[[Category: Svergun D]]

Current revision

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

PDB ID 3zgi

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