9HW9
Structural characterization of the type 3 fimbrial subunit MrkA from Klebsiella pneumoniae by solution NMR spectroscopy
Summary for 9HW9
| Entry DOI | 10.2210/pdb9hw9/pdb |
| NMR Information | BMRB: 52205 |
| Descriptor | Fimbrial subunit type 3 (1 entity in total) |
| Functional Keywords | protein antigen, klebsiella pneumoniae, self-complemented mrka monomer, type 3 fimbriae, solution nmr structure determination, biofilm formation, cell adhesion |
| Biological source | Klebsiella pneumoniae |
| Total number of polymer chains | 1 |
| Total formula weight | 20639.42 |
| Authors | |
| Primary citation | Monaci, V.,Oldrini, D.,Gasperini, G.,Banci, L.,Cantini, F.,Micoli, F. Biological and structural characterization of the Type 3 fimbrial subunit MrkA from Klebsiella pneumoniae. Protein Sci., 34:e70343-e70343, 2025 Cited by PubMed Abstract: 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. PubMed: 41118248DOI: 10.1002/pro.70343 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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