3F65

The F4 fimbrial chaperone FaeE does not self-cap its interactive surfaces

Summary for 3F65

• Entry DOI: 10.2210/pdb3f65/pdb
• Related: 3F6I 3F6L
• Descriptor: Chaperone protein faeE, (4S)-2-METHYL-2,4-PENTANEDIOL, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: immunoglobulin-like fold, cell projection, chaperone, fimbrium, immunoglobulin domain, periplasm, plasmid
• Biological source: Escherichia coli
• Cellular location: Periplasm: P25401
• Total number of polymer chains: 8
• Total formula weight: 198859.26

Authors

Van Molle, I.,Moonens, K.,Buts, L.,Garcia-Pino, A.,Wyns, L.,De Greve, H.,Bouckaert, J. (deposition date: 2008-11-05, release date: 2009-05-19, Last modification date: 2023-11-01)

• Primary citation: Van Molle, I.,Moonens, K.,Buts, L.,Garcia-Pino, A.,Panjikar, S.,Wyns, L.,De Greve, H.,Bouckaert, J.; The F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfaces; Acta Crystallogr.,Sect.D, 65:411-420, 2009; PubMed: 19390146; DOI: 10.1107/S0907444909005174

Experimental method

X-RAY DIFFRACTION (2.29 Å)