6h1x: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='6h1x' size='340' side='right' caption='[[6h1x]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='6h1x' size='340' side='right' caption='[[6h1x]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6h1x]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H1X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H1X FirstGlance]. <br> | <table><tr><td colspan='2'>[[6h1x]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Promh Promh]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H1X OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H1X FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PMI0533 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=529507 PROMH])</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=6h1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h1x OCA], [http://pdbe.org/6h1x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h1x RCSB], [http://www.ebi.ac.uk/pdbsum/6h1x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h1x 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=6h1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h1x OCA], [http://pdbe.org/6h1x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h1x RCSB], [http://www.ebi.ac.uk/pdbsum/6h1x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h1x ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The important uropathogen Proteus mirabilis encodes a record number of chaperone/usher-pathway adhesive fimbriae. Such fimbriae, which are used for adhesion to cell surfaces/tissues and for biofilm formation, are typically important virulence factors in bacterial pathogenesis. Here, the structures of the receptor-binding domains of the tip-located two-domain adhesins UcaD (1.5 A resolution) and AtfE (1.58 A resolution) from two P. mirabilis fimbriae (UCA/NAF and ATF) are presented. The structures of UcaD and AtfE are both similar to the F17G type of tip-located fimbrial receptor-binding domains, and the structures are very similar despite having only limited sequence similarity. These structures represent an important step towards a molecular-level understanding of P. mirabilis fimbrial adhesins and their roles in the complex pathogenesis of urinary-tract infections. | |||
Structures of two fimbrial adhesins, AtfE and UcaD, from the uropathogen Proteus mirabilis.,Jiang W, Ubhayasekera W, Pearson MM, Knight SD Acta Crystallogr D Struct Biol. 2018 Nov 1;74(Pt 11):1053-1062. doi:, 10.1107/S2059798318012391. Epub 2018 Oct 29. PMID:30387764<ref>PMID:30387764</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6h1x" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Promh]] | |||
[[Category: Knight, S D]] | [[Category: Knight, S D]] | ||
[[Category: Wangshu, J]] | [[Category: Wangshu, J]] | ||
Latest revision as of 12:04, 14 November 2018
Receptor-binding domain of Proteus mirabilis Uroepithelial Cell Adhesin UcaD21-211Receptor-binding domain of Proteus mirabilis Uroepithelial Cell Adhesin UcaD21-211
Structural highlights
Publication Abstract from PubMedThe important uropathogen Proteus mirabilis encodes a record number of chaperone/usher-pathway adhesive fimbriae. Such fimbriae, which are used for adhesion to cell surfaces/tissues and for biofilm formation, are typically important virulence factors in bacterial pathogenesis. Here, the structures of the receptor-binding domains of the tip-located two-domain adhesins UcaD (1.5 A resolution) and AtfE (1.58 A resolution) from two P. mirabilis fimbriae (UCA/NAF and ATF) are presented. The structures of UcaD and AtfE are both similar to the F17G type of tip-located fimbrial receptor-binding domains, and the structures are very similar despite having only limited sequence similarity. These structures represent an important step towards a molecular-level understanding of P. mirabilis fimbrial adhesins and their roles in the complex pathogenesis of urinary-tract infections. Structures of two fimbrial adhesins, AtfE and UcaD, from the uropathogen Proteus mirabilis.,Jiang W, Ubhayasekera W, Pearson MM, Knight SD Acta Crystallogr D Struct Biol. 2018 Nov 1;74(Pt 11):1053-1062. doi:, 10.1107/S2059798318012391. Epub 2018 Oct 29. PMID:30387764[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||