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| | <StructureSection load='6e55' size='340' side='right'caption='[[6e55]], [[Resolution|resolution]] 1.57Å' scene=''> | | <StructureSection load='6e55' size='340' side='right'caption='[[6e55]], [[Resolution|resolution]] 1.57Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6e55]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pneumoniae"_(schroeter_1886)_flugge_1886 "bacillus pneumoniae" (schroeter 1886) flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E55 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6e55]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E55 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">feoA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=573 "Bacillus pneumoniae" (Schroeter 1886) Flugge 1886])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.57Å</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=6e55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e55 OCA], [http://pdbe.org/6e55 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e55 RCSB], [http://www.ebi.ac.uk/pdbsum/6e55 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e55 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=6e55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e55 OCA], [https://pdbe.org/6e55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e55 RCSB], [https://www.ebi.ac.uk/pdbsum/6e55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e55 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/A6TF31_KLEP7 A6TF31_KLEP7] |
| - | In order to establish infection, pathogenic bacteria must obtain essential nutrients such as iron. Under acidic and/or anaerobic conditions, most bacteria utilize the Feo system in order to acquire ferrous iron (Fe(2+) ) from their host environment. The mechanism of this process, including its regulation, remains poorly understood. In this work, we have determined the crystal structure of FeoA from the nosocomial agent Klebsiella pneumoniae (KpFeoA). Our structure reveals an SH3-like domain that mediates interactions between neighboring polypeptides via hydrophobic intercalations into a Leu-rich surface ridge. Using docking of a small peptide corresponding to a postulated FeoB partner binding site, we demonstrate that KpFeoA can assume both "open" and "closed" conformations, controlled by binding at this Leu-rich ridge. We propose a model in which a "C-shaped" clamp along the FeoA surface mediates interactions with its partner protein, FeoB. These findings are the first to demonstrate atomic-level details of FeoA-based protein-protein interactions and provide a framework for testing FeoA-FeoB interactions, which could be exploited for future antibiotic developments.
| + | |
| - | | + | |
| - | The crystal structure of Klebsiella pneumoniae FeoA reveals a site for protein-protein interactions.,Linkous RO, Sestok AE, Smith AT Proteins. 2019 Jun 4. doi: 10.1002/prot.25755. PMID:31162843<ref>PMID:31162843</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6e55" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Klebsiella pneumoniae]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Linkous, R O]] | + | [[Category: Linkous RO]] |
| - | [[Category: Sestok, A E]] | + | [[Category: Sestok AE]] |
| - | [[Category: Smith, A T]] | + | [[Category: Smith AT]] |
| - | [[Category: Iron transport]]
| + | |
| - | [[Category: Protein regulation]]
| + | |
| - | [[Category: Protein-protein interaction]]
| + | |
| - | [[Category: Transport protein]]
| + | |
