5eq6: Difference between revisions
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<StructureSection load='5eq6' size='340' side='right' caption='[[5eq6]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='5eq6' size='340' side='right' caption='[[5eq6]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5eq6]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EQ6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5eq6]] 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=5EQ6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EQ6 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5eox|5eox]], [[5eoy|5eoy]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5eox|5eox]], [[5eoy|5eoy]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pilM, PA5044 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</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=5eq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eq6 OCA], [http://pdbe.org/5eq6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eq6 RCSB], [http://www.ebi.ac.uk/pdbsum/5eq6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5eq6 ProSAT]</span></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=5eq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eq6 OCA], [http://pdbe.org/5eq6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eq6 RCSB], [http://www.ebi.ac.uk/pdbsum/5eq6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5eq6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Pseae]] | |||
[[Category: Burrows, L L]] | [[Category: Burrows, L L]] | ||
[[Category: Calmettes, C]] | [[Category: Calmettes, C]] | ||
Revision as of 15:39, 6 November 2017
Pseudomonas aeruginosa PilM bound to AMP-PNPPseudomonas aeruginosa PilM bound to AMP-PNP
Structural highlights
Publication Abstract from PubMedPseudomonas aeruginosais an opportunistic bacterial pathogen that expresses type IVa pili (T4aP). The pilus assembly system, which promotes surface-associated twitching motility and virulence, is comprised of inner and outer membrane subcomplexes, connected by an alignment subcomplex composed of PilMNOP. PilM binds to the N-terminus of PilN, and we hypothesize that this interaction causes functionally significant structural changes in PilM. To characterize this interaction, we determined the crystal structures of PilM and a PilM chimera where PilM was fused to the first twelve residues of PilN (PilM:PilN1-12). Structural analysis, multi-angle light scattering coupled with size exclusion chromatography, and bacterial two-hybrid (BACTH) data revealed that PilM forms dimers mediated by the binding of a novel conserved motif in the N-terminus of PilM, and binding PilN abrogates this binding interface resulting in PilM monomerization. Structural comparison of PilM to PilM:PilN1-12 revealed that upon PilN binding there is a large domain closure in PilM that alters its ATP binding site. Using biolayer interferometry we found that the association rate of PilN to PilM is higher in the presence of ATP compared to ADP. BACTH data suggested the connectivity of the cytoplasmic and inner membrane components of the T4aP machinery inP. aeruginosa, with PilM binding to PilB, PilT, and PilC, in addition to PilN. Pull-down experiments demonstrated direct interactions of PilM with PilB and PilT. We propose a working model in which dynamic binding of PilN facilitates functionally relevant structural changes in PilM. PilN binding modulates the structure and binding partners of the Pseudomonas aeruginosa Type IVa Pilus protein PilM.,McCallum M, Tammam S, Little DJ, Robinson H, Koo J, Shah M, Calmettes C, Moraes TF, Burrows LL, Howell PL J Biol Chem. 2016 Mar 28. pii: jbc.M116.718353. PMID:27022027[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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