Structure determination of a protein assembly by amino acid selective cross-saturation.
Amino acid selective cross-saturation (ASCS) method not only provides information about the interface of a protein assembly by the spin relaxation experiment, but also identifies the amino acid residues in the acceptor protein, which are located close to the selectively labeled amino acid residues in the donor protein. Here, a new method was developed to build a precise structural model of a protein assembly, which satisfies the experimental ASCS values, using simulated annealing computation. This method was applied to the ubiquitin-yeast ubiquitin hydrolase 1 (Ub-YUH1) complex to build a precise complex structure compatible with that determined by X-ray crystallography.
Kanamori
Eiji
E
Japan Biological Informatics Consortium (JBIC), Koto-ku, Tokyo 135-0064, Japan. e-kanamori@aist.go.jp
Igarashi
Shunsuke
S
Osawa
Masanori
M
Fukunishi
Yoshifumi
Y
Shimada
Ichio
I
Nakamura
Haruki
H
D000465:Algorithms; D018360:Crystallography, X-Ray; D010450:Endopeptidases / Q000737:chemistry*; D005656:Fungal Proteins / Q000737:chemistry*; D056004:Molecular Dynamics Simulation; D011487:Protein Conformation; D054730:Protein Interaction Domains and Motifs; D025801:Ubiquitin / Q000737:chemistry*; D064570:Ubiquitin-Specific Proteases
D005656:Fungal Proteins; D025801:Ubiquitin; D010450:Endopeptidases; D064570:Ubiquitin-Specific Proteases