5oh0: Difference between revisions
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<StructureSection load='5oh0' size='340' side='right' caption='[[5oh0]], [[Resolution|resolution]] 4.20Å' scene=''> | <StructureSection load='5oh0' size='340' side='right' caption='[[5oh0]], [[Resolution|resolution]] 4.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5oh0]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OH0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OH0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5oh0]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OH0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OH0 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=5oh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oh0 OCA], [http://pdbe.org/5oh0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oh0 RCSB], [http://www.ebi.ac.uk/pdbsum/5oh0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oh0 ProSAT]</span></td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fimA, pilA, b4314, JW4277 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=5oh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oh0 OCA], [http://pdbe.org/5oh0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oh0 RCSB], [http://www.ebi.ac.uk/pdbsum/5oh0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oh0 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == 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. | [[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 == | |||
Adhesive chaperone-usher pili are long, supramolecular protein fibers displayed on the surface of many bacterial pathogens. The type 1 and P pili of uropathogenic Escherichia coli (UPEC) play important roles during urinary tract colonization, mediating attachment to the bladder and kidney, respectively. The biomechanical properties of the helical pilus rods allow them to reversibly uncoil in response to flow-induced forces, allowing UPEC to retain a foothold in the unique and hostile environment of the urinary tract. Here we provide the 4.2-A resolution cryo-EM structure of the type 1 pilus rod, which together with the previous P pilus rod structure rationalizes the remarkable "spring-like" properties of chaperone-usher pili. The cryo-EM structure of the type 1 pilus rod differs in its helical parameters from the structure determined previously by a hybrid approach. We provide evidence that these structural differences originate from different quaternary structures of pili assembled in vivo and in vitro. | |||
The Cryoelectron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod.,Hospenthal MK, Zyla D, Costa TRD, Redzej A, Giese C, Lillington J, Glockshuber R, Waksman G Structure. 2017 Nov 7. pii: S0969-2126(17)30332-5. doi:, 10.1016/j.str.2017.10.004. PMID:29129382<ref>PMID:29129382</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5oh0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ecoli]] | |||
[[Category: Costa, T R.D]] | [[Category: Costa, T R.D]] | ||
[[Category: Hospenthal, M K]] | [[Category: Hospenthal, M K]] | ||
Revision as of 10:30, 29 November 2017
The Cryo-Electron Microscopy Structure of the Type 1 Chaperone-Usher Pilus RodThe Cryo-Electron Microscopy Structure of the Type 1 Chaperone-Usher 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 PubMedAdhesive chaperone-usher pili are long, supramolecular protein fibers displayed on the surface of many bacterial pathogens. The type 1 and P pili of uropathogenic Escherichia coli (UPEC) play important roles during urinary tract colonization, mediating attachment to the bladder and kidney, respectively. The biomechanical properties of the helical pilus rods allow them to reversibly uncoil in response to flow-induced forces, allowing UPEC to retain a foothold in the unique and hostile environment of the urinary tract. Here we provide the 4.2-A resolution cryo-EM structure of the type 1 pilus rod, which together with the previous P pilus rod structure rationalizes the remarkable "spring-like" properties of chaperone-usher pili. The cryo-EM structure of the type 1 pilus rod differs in its helical parameters from the structure determined previously by a hybrid approach. We provide evidence that these structural differences originate from different quaternary structures of pili assembled in vivo and in vitro. The Cryoelectron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod.,Hospenthal MK, Zyla D, Costa TRD, Redzej A, Giese C, Lillington J, Glockshuber R, Waksman G Structure. 2017 Nov 7. pii: S0969-2126(17)30332-5. doi:, 10.1016/j.str.2017.10.004. PMID:29129382[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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