This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
5y9g
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='5y9g' size='340' side='right' caption='[[5y9g]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='5y9g' size='340' side='right' caption='[[5y9g]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5y9g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y9G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y9G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5y9g]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_enteritidis"_gaertner_1888 "bacillus enteritidis" gaertner 1888]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y9G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y9G 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=5y9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y9g OCA], [http://pdbe.org/5y9g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y9g RCSB], [http://www.ebi.ac.uk/pdbsum/5y9g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y9g ProSAT]</span></td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IN36_14140 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=149539 "Bacillus enteritidis" Gaertner 1888])</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=5y9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y9g OCA], [http://pdbe.org/5y9g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y9g RCSB], [http://www.ebi.ac.uk/pdbsum/5y9g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y9g ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pili are critical in host recognition, colonization and biofilm formation during bacterial infection. Here, we report the crystal structures of SafD-dsc and SafD-SafA-SafA (SafDAA-dsc) in Saf pili. Cell adherence assays show that SafD and SafA are both required for host recognition, suggesting a poly-adhesive mechanism for Saf pili. Moreover, the SafDAA-dsc structure, as well as SAXS characterization, reveals an unexpected inter-molecular oligomerization, prompting the investigation of Saf-driven self-association in biofilm formation. The bead/cell aggregation and biofilm formation assays are used to demonstrate the novel function of Saf pili. Structure-based mutants targeting the inter-molecular hydrogen bonds and complementary architecture/surfaces in SafDAA-dsc dimers significantly impaired the Saf self-association activity and biofilm formation. In summary, our results identify two novel functions of Saf pili: the poly-adhesive and self-associating activities. More importantly, Saf-Saf structures and functional characterizations help to define a pili-mediated inter-cellular oligomerizaiton mechanism for bacterial aggregation, colonization and ultimate biofilm formation. | ||
| + | |||
| + | Structural basis of host recognition and biofilm formation by Salmonella Saf pili.,Zeng L, Zhang L, Wang P, Meng G Elife. 2017 Nov 10;6. doi: 10.7554/eLife.28619. PMID:29125121<ref>PMID:29125121</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5y9g" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Bacillus enteritidis gaertner 1888]] | ||
[[Category: Meng, G]] | [[Category: Meng, G]] | ||
[[Category: Wang, P R]] | [[Category: Wang, P R]] | ||
Revision as of 07:58, 6 December 2017
Crystal structure of Salmonella SafD adhesin
| |||||||||||
