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| | ==Crystal structure of Pseudomonas aeruginosa PilY1 C-terminal domain== | | ==Crystal structure of Pseudomonas aeruginosa PilY1 C-terminal domain== |
| - | <StructureSection load='3hx6' size='340' side='right' caption='[[3hx6]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='3hx6' size='340' side='right'caption='[[3hx6]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3hx6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HX6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HX6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3hx6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HX6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HX6 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 2.1Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pilY1, PA4554 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=3hx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hx6 OCA], [http://pdbe.org/3hx6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hx6 RCSB], [http://www.ebi.ac.uk/pdbsum/3hx6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hx6 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=3hx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hx6 OCA], [https://pdbe.org/3hx6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hx6 RCSB], [https://www.ebi.ac.uk/pdbsum/3hx6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hx6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PILY1_PSEAE PILY1_PSEAE] Involved in pilus assembly, twitching motility and adhesion to host cells. Primes type IV pili (T4P) assembly and is required for inclusion of minor pilins PilV, PilW and PilX to the surface pili (PubMed:25389296). Stabilizes assembled pilus fibers likely by antagonizing retraction mediated by PilT. Calcium-binding and calcium release by PilY1 seem to be essential for twitching motility and for regulation of pilus retraction dynamics of PilT (By similarity).[UniProtKB:S0HPF7]<ref>PMID:25389296</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hx/3hx6_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hx/3hx6_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Orans, J]] | + | [[Category: Large Structures]] |
| - | [[Category: Redinbo, M R]] | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Beta propeller]] | + | [[Category: Orans J]] |
| - | [[Category: Cell adhesion]] | + | [[Category: Redinbo MR]] |
| - | [[Category: Pilus protein]]
| + | |
| Structural highlights
Function
PILY1_PSEAE Involved in pilus assembly, twitching motility and adhesion to host cells. Primes type IV pili (T4P) assembly and is required for inclusion of minor pilins PilV, PilW and PilX to the surface pili (PubMed:25389296). Stabilizes assembled pilus fibers likely by antagonizing retraction mediated by PilT. Calcium-binding and calcium release by PilY1 seem to be essential for twitching motility and for regulation of pilus retraction dynamics of PilT (By similarity).[UniProtKB:S0HPF7][1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Several bacterial pathogens require the "twitching" motility produced by filamentous type IV pili (T4P) to establish and maintain human infections. Two cytoplasmic ATPases function as an oscillatory motor that powers twitching motility via cycles of pilus extension and retraction. The regulation of this motor, however, has remained a mystery. We present the 2.1 A resolution crystal structure of the Pseudomonas aeruginosa pilus-biogenesis factor PilY1, and identify a single site on this protein required for bacterial translocation. The structure reveals a modified beta-propeller fold and a distinct EF-hand-like calcium-binding site conserved in pathogens with retractile T4P. We show that preventing calcium binding by PilY1 using either an exogenous calcium chelator or mutation of a single residue disrupts Pseudomonas twitching motility by eliminating surface pili. In contrast, placing a lysine in this site to mimic the charge of a bound calcium interferes with motility in the opposite manner-by producing an abundance of nonfunctional surface pili. Our data indicate that calcium binding and release by the unique loop identified in the PilY1 crystal structure controls the opposing forces of pilus extension and retraction. Thus, PilY1 is an essential, calcium-dependent regulator of bacterial twitching motility.
Crystal structure analysis reveals Pseudomonas PilY1 as an essential calcium-dependent regulator of bacterial surface motility.,Orans J, Johnson MD, Coggan KA, Sperlazza JR, Heiniger RW, Wolfgang MC, Redinbo MR Proc Natl Acad Sci U S A. 2009 Dec 28. PMID:20080557[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nguyen Y, Sugiman-Marangos S, Harvey H, Bell SD, Charlton CL, Junop MS, Burrows LL. Pseudomonas aeruginosa minor pilins prime type IVa pilus assembly and promote surface display of the PilY1 adhesin. J Biol Chem. 2015 Jan 2;290(1):601-11. PMID:25389296 doi:10.1074/jbc.M114.616904
- ↑ Orans J, Johnson MD, Coggan KA, Sperlazza JR, Heiniger RW, Wolfgang MC, Redinbo MR. Crystal structure analysis reveals Pseudomonas PilY1 as an essential calcium-dependent regulator of bacterial surface motility. Proc Natl Acad Sci U S A. 2009 Dec 28. PMID:20080557
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