3fhv: Difference between revisions
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<StructureSection load='3fhv' size='340' side='right'caption='[[3fhv]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='3fhv' size='340' side='right'caption='[[3fhv]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3fhv]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FHV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FHV FirstGlance]. <br> | <table><tr><td colspan='2'>[[3fhv]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhi Salmonella enterica subsp. enterica serovar Typhi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FHV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FHV FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAR:D-ARGININE'>DAR</scene>, <scene name='pdbligand=DGL:D-GLUTAMIC+ACID'>DGL</scene>, <scene name='pdbligand=DPR:D-PROLINE'>DPR</scene>, <scene name='pdbligand=DTY:D-TYROSINE'>DTY</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fhv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fhv OCA], [https://pdbe.org/3fhv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fhv RCSB], [https://www.ebi.ac.uk/pdbsum/3fhv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fhv ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fhv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fhv OCA], [https://pdbe.org/3fhv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fhv RCSB], [https://www.ebi.ac.uk/pdbsum/3fhv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fhv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8Z1L1_SALTI Q8Z1L1_SALTI] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Salmonella enterica subsp. enterica serovar Typhi]] | ||
[[Category: | [[Category: Balakrishna AM]] | ||
[[Category: | [[Category: Swaminathan K]] | ||
Revision as of 18:29, 1 November 2023
Structural basis of Salmonella typhi type IVb PilS and cystic fibrosis transmembrane conductance regulator (CFTR) interactionStructural basis of Salmonella typhi type IVb PilS and cystic fibrosis transmembrane conductance regulator (CFTR) interaction
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe type IVb pilus of the enteropathogenic bacteria Salmonella typhi is a major adhesion factor during the entry of this pathogen into gastrointestinal epithelial cells. Its target of adhesion is a stretch of 10 residues from the first extracellular domain of cystic fibrosis transmembrane conductance regulator (CFTR). The crystal structure of the N-terminal 25 amino acid deleted S. typhi native PilS protein (DeltaPilS), which makes the pilus, was determined at 1.9 A resolution by the multiwavelength anomalous dispersion method. Also, the structure of the complex of DeltaPilS and a target CFTR peptide, determined at 1.8 A, confirms that residues 113-117 (NKEER) of CFTR are involved in binding with the pilin protein and gives us insight on the amino acids that are essential for binding. Furthermore, we have also explored the role of a conserved disulfide bridge in pilus formation. The subunit structure and assembly architecture are crucial for understanding pilus functions and designing suitable therapeutics against typhoid. Structural basis of typhoid: Salmonella typhi type IVb pilin (PilS) and cystic fibrosis transmembrane conductance regulator interaction.,Balakrishna AM, Saxena AM, Mok HY, Swaminathan K Proteins. 2009 Nov 1;77(2):253-61. PMID:19626704[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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