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2rjz
From Proteopedia
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==Crystal structure of the type 4 fimbrial biogenesis protein PilO from Pseudomonas aeruginosa== | ==Crystal structure of the type 4 fimbrial biogenesis protein PilO from Pseudomonas aeruginosa== | ||
| - | <StructureSection load='2rjz' size='340' side='right' caption='[[2rjz]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='2rjz' size='340' side='right'caption='[[2rjz]], [[Resolution|resolution]] 2.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2rjz]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2rjz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RJZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RJZ FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rjz OCA], [https://pdbe.org/2rjz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rjz RCSB], [https://www.ebi.ac.uk/pdbsum/2rjz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rjz ProSAT], [https://www.topsan.org/Proteins/NYSGXRC/2rjz TOPSAN]</span></td></tr> |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q51353_PSEAI Q51353_PSEAI] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rj/2rjz_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rj/2rjz_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2rjz ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Type IV pili (T4P) are bacterial virulence factors responsible for attachment to surfaces and for twitching motility, a motion that involves a succession of pilus extension and retraction cycles. In the opportunistic pathogen Pseudomonas aeruginosa, the PilM/N/O/P proteins are essential for T4P biogenesis, and genetic and biochemical analyses strongly suggest that they form an inner-membrane complex. Here, we show through co-expression and biochemical analysis that the periplasmic domains of PilN and PilO interact to form a heterodimer. The structure of residues 69-201 of the periplasmic domain of PilO was determined to 2.2 A resolution and reveals the presence of a homodimer in the asymmetric unit. Each monomer consists of two N-terminal coiled coils and a C-terminal ferredoxin-like domain. This structure was used to generate homology models of PilN and the PilN/O heterodimer. Our structural analysis suggests that in vivo PilN/O heterodimerization would require changes in the orientation of the first N-terminal coiled coil, which leads to two alternative models for the role of the transmembrane domains in the PilN/O interaction. Analysis of PilN/O orthologues in the type II secretion system EpsL/M revealed significant similarities in their secondary structures and the tertiary structures of PilO and EpsM, although the way these proteins interact to form inner-membrane complexes appears to be different in T4P and type II secretion. Our analysis suggests that PilN interacts directly, via its N-terminal tail, with the cytoplasmic protein PilM. This work shows a direct interaction between the periplasmic domains of PilN and PilO, with PilO playing a key role in the proper folding of PilN. Our results suggest that PilN/O heterodimers form the foundation of the inner-membrane PilM/N/O/P complex, which is critical for the assembly of a functional T4P complex. | ||
| - | |||
| - | Periplasmic domains of Pseudomonas aeruginosa PilN and PilO form a stable heterodimeric complex.,Sampaleanu LM, Bonanno JB, Ayers M, Koo J, Tammam S, Burley SK, Almo SC, Burrows LL, Howell PL J Mol Biol. 2009 Nov 20;394(1):143-59. PMID:19857646<ref>PMID:19857646</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Pseudomonas aeruginosa | + | [[Category: Large Structures]] |
| - | [[Category: Almo | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Bain | + | [[Category: Almo SC]] |
| - | [[Category: Bonanno | + | [[Category: Bain KT]] |
| - | [[Category: Burley | + | [[Category: Bonanno JB]] |
| - | [[Category: Chang | + | [[Category: Burley SK]] |
| - | [[Category: Freeman | + | [[Category: Chang S]] |
| - | + | [[Category: Freeman J]] | |
| - | [[Category: Ozyurt | + | [[Category: Ozyurt S]] |
| - | [[Category: Sauder | + | [[Category: Sauder JM]] |
| - | [[Category: Smith | + | [[Category: Smith D]] |
| - | [[Category: Wasserman | + | [[Category: Wasserman S]] |
| - | + | ||
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Current revision
Crystal structure of the type 4 fimbrial biogenesis protein PilO from Pseudomonas aeruginosa
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Categories: Large Structures | Pseudomonas aeruginosa PAO1 | Almo SC | Bain KT | Bonanno JB | Burley SK | Chang S | Freeman J | Ozyurt S | Sauder JM | Smith D | Wasserman S

