9hw9
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structural characterization of the type 3 fimbrial subunit MrkA from Klebsiella pneumoniae by solution NMR spectroscopy== | |
| + | <StructureSection load='9hw9' size='340' side='right'caption='[[9hw9]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9hw9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9HW9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9HW9 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=9hw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9hw9 OCA], [https://pdbe.org/9hw9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9hw9 RCSB], [https://www.ebi.ac.uk/pdbsum/9hw9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9hw9 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FM3_KLEPN FM3_KLEPN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Klebsiella pneumoniae is a Gram-negative opportunistic pathogen responsible for a wide range of community-associated and hospital-acquired infections and a major cause of neonatal sepsis in low- and middle-income countries. The pathogen's surface fimbriae, particularly the Type 3 fimbriae, are critical for bacterial adhesion, biofilm formation, and host defense evasion. MrkA, the pathogen's major Type 3 fimbrial subunit, has a structural function in fimbrial assembly, but its three-dimensional structure remains to be fully elucidated. In this study, we utilized solution-state nuclear magnetic resonance spectroscopy to elucidate the structure of MrkA, leveraging previously reported chemical shift assignments of a designed self-complementing monomeric protein. Additionally, we confirmed the ability of monoclonal antibodies, capable of recognizing MrkA oligomers on wild-type Klebsiella bacteria, to bind the recombinant MrkA protein. Our findings contribute to the evaluation of MrkA as a potential target in vaccine development against Klebsiella pneumoniae infections. | ||
| - | + | Biological and structural characterization of the Type 3 fimbrial subunit MrkA from Klebsiella pneumoniae.,Monaci V, Oldrini D, Gasperini G, Banci L, Cantini F, Micoli F Protein Sci. 2025 Nov;34(11):e70343. doi: 10.1002/pro.70343. PMID:41118248<ref>PMID:41118248</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9hw9" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Klebsiella pneumoniae]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cantini F]] | ||
| + | [[Category: Monaci V]] | ||
Current revision
Structural characterization of the type 3 fimbrial subunit MrkA from Klebsiella pneumoniae by solution NMR spectroscopy
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