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5LND

Crystal structure of self-complemented MyfA, the major subunit of Myf fimbriae from Yersinia enterocolitica

Summary for 5LND
Entry DOI10.2210/pdb5lnd/pdb
DescriptorFimbrial protein MyfA,Fimbrial protein MyfA,Fimbrial protein MyfA (2 entities in total)
Functional Keywordsig-like fold, beta sandwich, donor-strand complementation, cell adhesion
Biological sourceYersinia enterocolitica
More
Total number of polymer chains2
Total formula weight29285.55
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 citationPakharukova, 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: 27507539
DOI: 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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