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| | <StructureSection load='2ope' size='340' side='right'caption='[[2ope]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='2ope' size='340' side='right'caption='[[2ope]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ope]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"diplokokkus_intracellularis_meningitidis"_(sic)_weichselbaum_1887 "diplokokkus intracellularis meningitidis" (sic) weichselbaum 1887]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OPE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ope]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OPE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OPE FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2pil|2pil]], [[2hi2|2hi2]], [[2opd|2opd]]</div></td></tr> | + | </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=2ope FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ope OCA], [https://pdbe.org/2ope PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ope RCSB], [https://www.ebi.ac.uk/pdbsum/2ope PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ope ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pilX ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=487 "Diplokokkus intracellularis meningitidis" (sic) Weichselbaum 1887])</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=2ope FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ope OCA], [https://pdbe.org/2ope PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ope RCSB], [https://www.ebi.ac.uk/pdbsum/2ope PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ope ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dyer, D H]] | + | [[Category: Neisseria meningitidis]] |
| - | [[Category: Forest, K T]] | + | [[Category: Dyer DH]] |
| - | [[Category: Helaine, S]] | + | [[Category: Forest KT]] |
| - | [[Category: Pelicic, V]] | + | [[Category: Helaine S]] |
| - | [[Category: Adhesion]] | + | [[Category: Pelicic V]] |
| - | [[Category: Aggregation]]
| + | |
| - | [[Category: Bacterial pathogenesis]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Filament]]
| + | |
| - | [[Category: Minor pilin]]
| + | |
| - | [[Category: Neisseria meningitidi]]
| + | |
| - | [[Category: Pilx]]
| + | |
| - | [[Category: Type iv pilin]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Type IV pili (Tfp) are widespread filamentous bacterial organelles that mediate multiple virulence-related phenotypes. They are composed mainly of pilin subunits, which are processed before filament assembly by dedicated prepilin peptidases. Other proteins processed by these peptidases, whose molecular nature and mode of action remain enigmatic, play critical roles in Tfp biology. We have performed a detailed structure/function analysis of one such protein, PilX from Neisseria meningitidis, which is crucial for formation of bacterial aggregates and adhesion to human cells. The x-ray crystal structure of PilX reveals the alpha/beta roll fold shared by all pilins, and we show that this protein colocalizes with Tfp. These observations suggest that PilX is a minor, or low abundance, pilin that assembles within the filaments in a similar way to pilin. Deletion of a PilX distinctive structural element, which is predicted to be exposed on the filament surface, abolishes aggregation and adhesion. Our results support a model in which surface-exposed motifs in PilX subunits stabilize bacterial aggregates against the disruptive force of pilus retraction and illustrate how a minor pilus component can enhance the functional properties of pili of rather simple composition and structure.
3D structure/function analysis of PilX reveals how minor pilins can modulate the virulence properties of type IV pili.,Helaine S, Dyer DH, Nassif X, Pelicic V, Forest KT Proc Natl Acad Sci U S A. 2007 Oct 2;104(40):15888-93. Epub 2007 Sep 24. PMID:17893339[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Helaine S, Dyer DH, Nassif X, Pelicic V, Forest KT. 3D structure/function analysis of PilX reveals how minor pilins can modulate the virulence properties of type IV pili. Proc Natl Acad Sci U S A. 2007 Oct 2;104(40):15888-93. Epub 2007 Sep 24. PMID:17893339 doi:http://dx.doi.org/0707581104
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