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==Crystal structure of the KRT10-binding region domain of the pneumococcal serine rich repeat protein PsrP== | |||
<StructureSection load='3zgi' size='340' side='right' caption='[[3zgi]], [[Resolution|resolution]] 2.25Å' 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> | |||
</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> | |||
<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='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'>[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://www.rcsb.org/pdb/explore.do?structureId=3zgi RCSB], [http://www.ebi.ac.uk/pdbsum/3zgi PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:24430336</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
[[Category: Achour, A | == References == | ||
[[Category: Diamante, A | <references/> | ||
[[Category: Ebel, C | __TOC__ | ||
[[Category: Henriques-Normark, B | </StructureSection> | ||
[[Category: Hentrich, K | [[Category: Strpn]] | ||
[[Category: Kikhney, A | [[Category: Achour, A]] | ||
[[Category: Loefling, J | [[Category: Diamante, A]] | ||
[[Category: Mikaelsson, C | [[Category: Ebel, C]] | ||
[[Category: Normark, S | [[Category: Henriques-Normark, B]] | ||
[[Category: Schulte, T | [[Category: Hentrich, K]] | ||
[[Category: Svergun, D | [[Category: Kikhney, A]] | ||
[[Category: Loefling, J]] | |||
[[Category: Mikaelsson, C]] | |||
[[Category: Normark, S]] | |||
[[Category: Schulte, T]] | |||
[[Category: Svergun, D]] | |||
[[Category: Adhesin]] | [[Category: Adhesin]] | ||
[[Category: Keratin-10]] | [[Category: Keratin-10]] | ||
[[Category: Srrp]] | [[Category: Srrp]] | ||
[[Category: Structural protein]] | [[Category: Structural protein]] | ||
Revision as of 20:01, 21 December 2014
Crystal structure of the KRT10-binding region domain of the pneumococcal serine rich repeat protein PsrPCrystal structure of the KRT10-binding region domain of the pneumococcal serine rich repeat protein PsrP
Structural highlights
Publication Abstract from PubMedStreptococcus 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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