1K53

Monomeric Protein L B1 Domain with a G15A Mutation

Summary for 1K53

• Entry DOI: 10.2210/pdb1k53/pdb
• Related: 1HZ5 1HZ6 1K50 1K51 1K52
• Descriptor: Protein L, ZINC ION (3 entities in total)
• Functional Keywords: protein l b1 domain, strained beta-hairpin turn, positive phi angles, domain swapping, amyloid formation, protein binding
• Biological source: Finegoldia magna
• Total number of polymer chains: 2
• Total formula weight: 16657.14

Authors

O'Neill, J.W.,Kim, D.E.,Johnsen, K.,Baker, D.,Zhang, K.Y.J. (deposition date: 2001-10-09, release date: 2001-12-05, Last modification date: 2023-08-16)

Primary citation

O'Neill, J.W.,Kim, D.E.,Johnsen, K.,Baker, D.,Zhang, K.Y.
Single-site mutations induce 3D domain swapping in the B1 domain of protein L from Peptostreptococcus magnus.
Structure, 9:1017-1027, 2001

PubMed Abstract: Thermodynamic and kinetic studies of the Protein L B1 domain (Ppl) suggest a folding pathway in which, during the folding transition, the first beta hairpin is formed while the second beta hairpin and the alpha helix are largely unstructured. The same mutations in the two beta turns have opposite effects on the folding and unfolding rates. Three of the four residues composing the second beta turn in Ppl have consecutive positive phi angles, indicating strain in the second beta turn.

PubMed: 11709166
DOI: 10.1016/S0969-2126(01)00667-0

Experimental method

X-RAY DIFFRACTION (2.1 Å)