6c53: Difference between revisions
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==Cryo-EM structure of the Type 1 pilus rod== | |||
<StructureSection load='6c53' size='340' side='right' caption='[[6c53]], [[Resolution|resolution]] 4.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6c53]] is a 11 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C53 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C53 FirstGlance]. <br> | |||
</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=6c53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c53 OCA], [http://pdbe.org/6c53 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c53 RCSB], [http://www.ebi.ac.uk/pdbsum/6c53 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c53 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/FIMA1_ECOLI FIMA1_ECOLI]] Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Uropathogenic E. coli (UPEC), which cause urinary tract infections (UTI), utilize type 1 pili, a chaperone usher pathway (CUP) pilus, to cause UTI and colonize the gut. The pilus rod, comprised of repeating FimA subunits, provides a structural scaffold for displaying the tip adhesin, FimH. We solved the 4.2 A resolution structure of the type 1 pilus rod using cryo-electron microscopy. Residues forming the interactive surfaces that determine the mechanical properties of the rod were maintained by selection based on a global alignment of fimA sequences. We identified mutations that did not alter pilus production in vitro but reduced the force required to unwind the rod. UPEC expressing these mutant pili were significantly attenuated in bladder infection and intestinal colonization in mice. This study elucidates an unappreciated functional role for the molecular spring-like property of type 1 pilus rods in host-pathogen interactions and carries important implications for other pilus-mediated diseases. | |||
Functional role of the type 1 pilus rod structure in mediating host-pathogen interactions.,Spaulding CN, Schreiber HL, Zheng W, Dodson KW, Hazen JE, Conover MS, Wang F, Svenmarker P, Luna-Rico A, Francetic O, Andersson M, Hultgren S, Egelman EH Elife. 2018 Jan 18;7. pii: 31662. doi: 10.7554/eLife.31662. PMID:29345620<ref>PMID:29345620</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6c53" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Egelman, E H]] | |||
[[Category: Francetic, O]] | |||
[[Category: Hultgren, S J]] | |||
[[Category: Luna-Rico, A]] | |||
[[Category: Wang, F]] | |||
[[Category: Zheng, W]] | |||
[[Category: Adhesive pili]] | |||
[[Category: Helical rod]] | |||
[[Category: Protein fibril]] | |||
[[Category: Type 1 pili]] | |||
Revision as of 08:59, 31 January 2018
Cryo-EM structure of the Type 1 pilus rodCryo-EM structure of the Type 1 pilus rod
Structural highlights
Function[FIMA1_ECOLI] Fimbriae (also called pili), polar filaments radiating from the surface of the bacterium to a length of 0.5-1.5 micrometers and numbering 100-300 per cell, enable bacteria to colonize the epithelium of specific host organs. Publication Abstract from PubMedUropathogenic E. coli (UPEC), which cause urinary tract infections (UTI), utilize type 1 pili, a chaperone usher pathway (CUP) pilus, to cause UTI and colonize the gut. The pilus rod, comprised of repeating FimA subunits, provides a structural scaffold for displaying the tip adhesin, FimH. We solved the 4.2 A resolution structure of the type 1 pilus rod using cryo-electron microscopy. Residues forming the interactive surfaces that determine the mechanical properties of the rod were maintained by selection based on a global alignment of fimA sequences. We identified mutations that did not alter pilus production in vitro but reduced the force required to unwind the rod. UPEC expressing these mutant pili were significantly attenuated in bladder infection and intestinal colonization in mice. This study elucidates an unappreciated functional role for the molecular spring-like property of type 1 pilus rods in host-pathogen interactions and carries important implications for other pilus-mediated diseases. Functional role of the type 1 pilus rod structure in mediating host-pathogen interactions.,Spaulding CN, Schreiber HL, Zheng W, Dodson KW, Hazen JE, Conover MS, Wang F, Svenmarker P, Luna-Rico A, Francetic O, Andersson M, Hultgren S, Egelman EH Elife. 2018 Jan 18;7. pii: 31662. doi: 10.7554/eLife.31662. PMID:29345620[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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