2rjz

<StructureSection load='2rjz' size='340' side='right' caption='[[2rjz]], [[Resolution|resolution]] 2.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[2rjz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RJZ FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2rjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rjz OCA], [http://pdbe.org/2rjz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rjz RCSB], [http://www.ebi.ac.uk/pdbsum/2rjz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rjz ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/2rjz TOPSAN]</span></td></tr>

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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2rjz" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Pseae]]

[[Category: Almo, S C]]

[[Category: Bain, K T]]

[[Category: Bonanno, J B]]

[[Category: Burley, S K]]

[[Category: Chang, S]]

[[Category: Freeman, J]]

[[Category: Structural genomic]]

[[Category: Ozyurt, S]]

[[Category: Sauder, J M]]

[[Category: Smith, D]]

[[Category: Wasserman, S]]

[[Category: Unknown function]]