1K51

A G55A Mutation Induces 3D Domain Swapping in the B1 Domain of Protein L from Peptostreptococcus magnus

Summary for 1K51

Entry DOI	10.2210/pdb1k51/pdb
Related	1hz5 1hz6 1JML 1K50 1K52 1K53
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	1
Total formula weight	8263.16
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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.8 Å)

Structure validation