2c4b
INHIBITOR CYSTINE KNOT PROTEIN MCOEETI FUSED TO THE CATALYTICALLY INACTIVE BARNASE MUTANT H102A
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OverviewOverview
We present a fusion system suited to determine the crystal structure of, small disulfide-rich proteins. McoEeTI, a hybrid inhibitor cystine knot, microprotein, was produced as a soluble fusion to a catalytically inactive, variant of the RNAse barnase in Escherichia coli. Functioning as a, versatile tag, barnase facilitated purification, crystallization and, high-resolution structure determination. Flexibility of the linker region, allows for different relative orientations of barnase and the fusion, partner in two crystallographically independent molecules and may thereby, facilitate crystal packing. Nevertheless, the linker region is well, ordered in both molecules. This system may prove more generally useful to, determine the crystal structure of peptides and small proteins.
About this StructureAbout this Structure
2C4B is a [Single protein] structure of sequence from [Bacillus amyloliquefaciens, momordica cochinchinensis, ecballium elaterium] with SO4, 2PE, EDO, MES, UNX, GOL and FMT as [ligands]. Active as [[1]], with EC number [3.1.27.3]. Full crystallographic information is available from [OCA].
ReferenceReference
Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI., Niemann HH, Schmoldt HU, Wentzel A, Kolmar H, Heinz DW, J Mol Biol. 2006 Feb 10;356(1):1-8. Epub 2005 Nov 21. PMID:16337652
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