Journal
PROTEIN SCIENCE
Volume 25, Issue 3, Pages 559-571Publisher
WILEY-BLACKWELL
DOI: 10.1002/pro.2863
Keywords
chaperone-assisted crystallization; crystallization chaperone; crystallization tag; maltose-binding protein; MBP fusion protein; surface entropy reduction mutagenesis
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Funding
- Intramural Research Program of the NIH, National Cancer Institute, Center for Cancer Research
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Although chaperone-assisted protein crystallization remains a comparatively rare undertaking, the number of crystal structures of polypeptides fused to maltose-binding protein (MBP) that have been deposited in the Protein Data Bank (PDB) has grown dramatically during the past decade. Altogether, 102 fusion protein structures were detected by Basic Local Alignment Search Tool (BLAST) analysis. Collectively, these structures comprise a range of sizes, space groups, and resolutions that are typical of the PDB as a whole. While most of these MBP fusion proteins were equipped with short inter-domain linkers to increase their rigidity, fusion proteins with long linkers have also been crystallized. In some cases, surface entropy reduction mutations in MBP appear to have facilitated the formation of crystals. A comparison of the structures of fused and unfused proteins, where both are available, reveals that MBP-mediated structural distortions are very rare.
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