6WVF

E.coli DsbB C104S with ubiquinone

Summary for 6WVF

• Entry DOI: 10.2210/pdb6wvf/pdb
• Descriptor: Green fluorescent protein,Disulfide bond formation protein B,Green fluorescent protein, UBIQUINONE-1 (3 entities in total)
• Functional Keywords: disulfide bond formation protein b(dsbb), disulfide bond, disulfide oxidoreductase, membrane protein
• Biological source: Aequorea victoria (Jellyfish); More
• Total number of polymer chains: 1
• Total formula weight: 45658.36

Authors

Liu, S.,Li, W. (deposition date: 2020-05-05, release date: 2021-01-13, Last modification date: 2024-11-13)

Primary citation

Liu, S.,Li, S.,Yang, Y.,Li, W.
Termini restraining of small membrane proteins enables structure determination at near-atomic resolution.
Sci Adv, 6:-, 2020

PubMed Abstract: Small membrane proteins are difficult targets for structural characterization. Here, we stabilize their folding by restraining their amino and carboxyl termini with associable protein entities, exemplified by the two halves of a superfolder GFP. The termini-restrained proteins are functional and show improved stability during overexpression and purification. The reassembled GFP provides a versatile scaffold for membrane protein crystallization, enables diffraction to atomic resolution, and facilitates crystal identification, phase determination, and density modification. This strategy gives rise to 14 new structures of five vertebrate proteins from distinct functional families, bringing a substantial expansion to the structural database of small membrane proteins. Moreover, a high-resolution structure of bacterial DsbB reveals that this thiol oxidoreductase is activated through a catalytic triad, similar to cysteine proteases. Overall, termini restraining proves exceptionally effective for stabilization and structure determination of small membrane proteins.

PubMed: 33355146
DOI: 10.1126/sciadv.abe3717

Experimental method

X-RAY DIFFRACTION (2.9 Å)