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| | <StructureSection load='3rpk' size='340' side='right'caption='[[3rpk]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='3rpk' size='340' side='right'caption='[[3rpk]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3rpk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"diplococcus_pneumoniae"_(klein_1884)_weichselbaum_1886 "diplococcus pneumoniae" (klein 1884) weichselbaum 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RPK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RPK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3rpk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RPK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RPK FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2l4o|2l4o]], [[2x9w|2x9w]], [[2x9x|2x9x]], [[2x9y|2x9y]], [[2x9z|2x9z]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rrgB ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 "Diplococcus pneumoniae" (Klein 1884) Weichselbaum 1886])</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=3rpk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rpk OCA], [https://pdbe.org/3rpk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rpk RCSB], [https://www.ebi.ac.uk/pdbsum/3rpk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rpk 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=3rpk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rpk OCA], [https://pdbe.org/3rpk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rpk RCSB], [https://www.ebi.ac.uk/pdbsum/3rpk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rpk ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0H2UNM7_STRPN A0A0H2UNM7_STRPN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 3rpk" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3rpk" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Pilin 3D structures|Pilin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Baker, E N]] | + | [[Category: Streptococcus pneumoniae]] |
| - | [[Category: Paterson, N G]] | + | [[Category: Baker EN]] |
| - | [[Category: Cell adhesion]] | + | [[Category: Paterson NG]] |
| - | [[Category: Cell wall]]
| + | |
| - | [[Category: Ig-like fold]]
| + | |
| - | [[Category: Isopeptide bond]]
| + | |
| - | [[Category: Peptidoglycan-anchor]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| Structural highlights
Function
A0A0H2UNM7_STRPN
Publication Abstract from PubMed
The surface of the pneumococcal cell is adorned with virulence factors including pili. The major pilin RrgB, which forms the pilus shaft on pathogenic Streptococcus pneumoniae, comprises four immunoglobulin (Ig)-like domains, each with a common CnaB topology. The three C-terminal domains are each stabilized by internal Lys-Asn isopeptide bonds, formed autocatalytically with the aid of an essential Glu residue. The structure and orientation of the crucial N-terminal domain, which provides the covalent linkage to the next pilin subunit in the shaft, however, remain incompletely characterised. We report the crystal structure of full length RrgB, solved by X-ray crystallography at 2.8 A resolution. The N-terminal (D1) domain makes few contacts with the rest of the RrgB structure, and has higher B-factors. This may explain why D1 is readily lost by proteolysis, as are the N-terminal domains of many major pilins. D1 is also found to have a triad of Lys, Asn and Glu residues in the same topological positions as in the other domains, yet mass spectrometry and the crystal structure show that no internal isopeptide bond is formed. We show that this is because beta-strand G of D1, which carries the Asn residue, diverges from beta-strand A, carrying the Lys residue, such that these residues are too far apart for bond formation. Strand G also carries the YPKN motif that provides the essential Lys residue for the sortase-mediated intermolecular linkages along the pilus shaft. Interaction with the sortase and formation of the intermolecular linkage could result in a change in the orientation of this strand, explaining why isopeptide bond formation in the N-terminal domains of some major pilins appears to take place only upon assembly of the pili.
Structure of the Full-Length Major Pilin from Streptococcus pneumoniae: Implications for Isopeptide Bond Formation in Gram-Positive Bacterial Pili.,Paterson NG, Baker EN PLoS One. 2011;6(7):e22095. Epub 2011 Jul 8. PMID:21760959[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Paterson NG, Baker EN. Structure of the Full-Length Major Pilin from Streptococcus pneumoniae: Implications for Isopeptide Bond Formation in Gram-Positive Bacterial Pili. PLoS One. 2011;6(7):e22095. Epub 2011 Jul 8. PMID:21760959 doi:10.1371/journal.pone.0022095
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