5LND
Crystal structure of self-complemented MyfA, the major subunit of Myf fimbriae from Yersinia enterocolitica
Summary for 5LND
Entry DOI | 10.2210/pdb5lnd/pdb |
Descriptor | Fimbrial protein MyfA,Fimbrial protein MyfA,Fimbrial protein MyfA (2 entities in total) |
Functional Keywords | ig-like fold, beta sandwich, donor-strand complementation, cell adhesion |
Biological source | Yersinia enterocolitica More |
Total number of polymer chains | 2 |
Total formula weight | 29285.55 |
Authors | Pakharukova, N.A.,Roy, S.,Tuitilla, M.,Zavialov, A.V. (deposition date: 2016-08-04, release date: 2016-08-24, Last modification date: 2016-11-30) |
Primary citation | Pakharukova, N.,Roy, S.,Tuittila, M.,Rahman, M.M.,Paavilainen, S.,Ingars, A.K.,Skaldin, M.,Lamminmaki, U.,Hard, T.,Teneberg, S.,Zavialov, A.V. Structural basis for Myf and Psa fimbriae-mediated tropism of pathogenic strains of Yersinia for host tissues. Mol.Microbiol., 102:593-610, 2016 Cited by PubMed: 27507539DOI: 10.1111/mmi.13481 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.46 Å) |
Structure validation
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