3WYQ

Crystal structure of the low-immunogenic core streptavidin mutant LISA-314 (Y22S/Y83S/R84K/E101D/R103K/E116N) at 1.0 A resolution

Summary for 3WYQ

• Entry DOI: 10.2210/pdb3wyq/pdb
• Related: 3WYP
• Descriptor: Streptavidin, BIOTIN, GLYCEROL, ... (5 entities in total)
• Functional Keywords: beta-barrel, biotin binding protein
• Biological source: Streptomyces avidinii
• Cellular location: Secreted: P22629
• Total number of polymer chains: 2
• Total formula weight: 27593.78

Authors

Kawato, T.,Mizohata, E.,Meshizuka, T.,Doi, H.,Kawamura, T.,Matsumura, H.,Yumura, K.,Tsumoto, K.,Kodama, T.,Inoue, T.,Sugiyama, A. (deposition date: 2014-09-05, release date: 2014-12-24, Last modification date: 2024-05-29)

Primary citation

Kawato, T.,Mizohata, E.,Meshizuka, T.,Doi, H.,Kawamura, T.,Matsumura, H.,Yumura, K.,Tsumoto, K.,Kodama, T.,Inoue, T.,Sugiyama, A.
Crystal structure of streptavidin mutant with low immunogenicity.
J.Biosci.Bioeng., 119:642-647, 2015

PubMed Abstract: We previously created a low-immunogenic core streptavidin mutant No. 314 (LISA-314) by replacing six amino-acid residues for use as a delivery tool for an antibody multistep pre-targeting process (Yumura et al., Protein Sci., 22, 213-221, 2013). Here, we performed high-resolution X-ray structural analyses of LISA-314 and wild-type streptavidin to investigate the effect of substitutions on the protein function and the three-dimensional structure. LISA-314 forms a tetramer in the same manner as wild-type streptavidin. The binding mode of d-biotin in LISA-314 is also completely identical to that in wild-type streptavidin, and conformational changes were observed mostly at the side chains of substituted sites. Any large conformational changes corresponding to the reduction of B factors around the substituted sites were not observed. These results demonstrated the LISA-314 acquired low immunogenicity without losing structural properties of original wild-type streptavidin.

PubMed: 25434833
DOI: 10.1016/j.jbiosc.2014.10.025

Experimental method

X-RAY DIFFRACTION (1 Å)