2lc4: Difference between revisions
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==Solution Structure of PilP from Pseudomonas aeruginosa== | ==Solution Structure of PilP from Pseudomonas aeruginosa== | ||
<StructureSection load='2lc4' size='340' side='right' caption='[[2lc4 | <StructureSection load='2lc4' size='340' side='right'caption='[[2lc4]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
[[2lc4]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2lc4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LC4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LC4 FirstGlance]. <br> | ||
<b> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
<b>Resources:</b> <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=2lc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lc4 OCA], [https://pdbe.org/2lc4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lc4 RCSB], [https://www.ebi.ac.uk/pdbsum/2lc4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lc4 ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q51354_PSEAI Q51354_PSEAI] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Type IVa pili are bacterial nanomachines required for colonization of surfaces, but little is known about the organization of proteins in this system. The Pseudomonas aeruginosa pilMNOPQ operon encodes five key members of the transenvelope complex facilitating pilus function. While PilQ forms the outer membrane secretin pore, the functions of the inner membrane-associated proteins PilM/N/O/P are less well defined. Structural characterization of a stable C-terminal fragment of PilP (PilP(Delta71) ) by NMR revealed a modified beta-sandwich fold, similar to that of Neisseria meningitidis PilP, although complementation experiments showed that the two proteins are not interchangeable likely due to divergent surface properties. PilP is an inner membrane putative lipoprotein, but mutagenesis of the putative lipobox had no effect on the localization and function of PilP. A larger fragment, PilP(Delta18-6His) , co-purified with a PilN(Delta44) /PilO(Delta51) heterodimer as a stable complex that eluted from a size exclusion chromatography column as a single peak with a molecular weight equivalent to two heterotrimers with 1:1:1 stoichiometry. Although PilO forms both homodimers and PilN-PilO heterodimers, PilP(Delta18-6His) did not interact stably with PilO(Delta51) alone. Together these data demonstrate that PilN/PilO/PilP interact directly to form a stable heterotrimeric complex, explaining the dispensability of PilP's lipid anchor for localization and function. | Type IVa pili are bacterial nanomachines required for colonization of surfaces, but little is known about the organization of proteins in this system. The Pseudomonas aeruginosa pilMNOPQ operon encodes five key members of the transenvelope complex facilitating pilus function. While PilQ forms the outer membrane secretin pore, the functions of the inner membrane-associated proteins PilM/N/O/P are less well defined. Structural characterization of a stable C-terminal fragment of PilP (PilP(Delta71) ) by NMR revealed a modified beta-sandwich fold, similar to that of Neisseria meningitidis PilP, although complementation experiments showed that the two proteins are not interchangeable likely due to divergent surface properties. PilP is an inner membrane putative lipoprotein, but mutagenesis of the putative lipobox had no effect on the localization and function of PilP. A larger fragment, PilP(Delta18-6His) , co-purified with a PilN(Delta44) /PilO(Delta51) heterodimer as a stable complex that eluted from a size exclusion chromatography column as a single peak with a molecular weight equivalent to two heterotrimers with 1:1:1 stoichiometry. Although PilO forms both homodimers and PilN-PilO heterodimers, PilP(Delta18-6His) did not interact stably with PilO(Delta51) alone. Together these data demonstrate that PilN/PilO/PilP interact directly to form a stable heterotrimeric complex, explaining the dispensability of PilP's lipid anchor for localization and function. | ||
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Characterization of the PilN, PilO and PilP type IVa pilus subcomplex.,Tammam S, Sampaleanu LM, Koo J, Sundaram P, Ayers M, Andrew Chong P, Forman-Kay JD, Burrows LL, Howell PL Mol Microbiol. 2011 Dec;82(6):1496-514. doi:, 10.1111/j.1365-2958.2011.07903.x. Epub 2011 Nov 18. PMID:22053789<ref>PMID:22053789</ref> | Characterization of the PilN, PilO and PilP type IVa pilus subcomplex.,Tammam S, Sampaleanu LM, Koo J, Sundaram P, Ayers M, Andrew Chong P, Forman-Kay JD, Burrows LL, Howell PL Mol Microbiol. 2011 Dec;82(6):1496-514. doi:, 10.1111/j.1365-2958.2011.07903.x. Epub 2011 Nov 18. PMID:22053789<ref>PMID:22053789</ref> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 2lc4" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Chong | [[Category: Chong P]] | ||
[[Category: Forman-Kay | [[Category: Forman-Kay JD]] | ||
[[Category: Howell | [[Category: Howell P]] | ||
[[Category: Tammam | [[Category: Tammam S]] | ||
Latest revision as of 05:41, 15 May 2024
Solution Structure of PilP from Pseudomonas aeruginosa
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