6D66

Crystal structure of the human dual specificity 1 catalytic domain (C258S) as a maltose binding protein fusion in complex with the designed AR protein mbp3_16

Summary for 6D66

• Entry DOI: 10.2210/pdb6d66/pdb
• Descriptor: Maltose-binding periplasmic protein,Dual specificity protein phosphatase 1, Designed AR protein mbp3_16, DI(HYDROXYETHYL)ETHER, ... (10 entities in total)
• Functional Keywords: dusp, c258s, hydrolase, mbp, darpin
• Biological source: Escherichia coli (strain K12); More
• Total number of polymer chains: 2
• Total formula weight: 74008.31

Authors

Gumpena, R.,Waugh, D.S.,Lountos, G.T. (deposition date: 2018-04-20, release date: 2018-09-19, Last modification date: 2023-10-04)

Primary citation

Gumpena, R.,Lountos, G.T.,Waugh, D.S.
MBP-binding DARPins facilitate the crystallization of an MBP fusion protein.
Acta Crystallogr F Struct Biol Commun, 74:549-557, 2018

PubMed Abstract: The production of high-quality crystals is the main bottleneck in determining the structures of proteins using X-ray crystallography. In addition to being recognized as a very effective solubility-enhancing fusion partner, Escherichia coli maltose-binding protein (MBP) has also been successfully employed as a `fixed-arm' crystallization chaperone in more than 100 cases. Here, it is reported that designed ankyrin-repeat proteins (DARPins) that bind with high affinity to MBP can promote the crystallization of an MBP fusion protein when the fusion protein alone fails to produce diffraction-quality crystals. As a proof of principle, three different co-crystal structures of MBP fused to the catalytic domain of human dual-specificity phosphatase 1 in complex with DARPins are reported.

PubMed: 30198887
DOI: 10.1107/S2053230X18009901

Experimental method

X-RAY DIFFRACTION (2.226 Å)