2c4b
From Proteopedia
Inhibitor cystine knot protein McoEeTI fused to the catalytically inactive barnase mutant H102A
Structural highlights
FunctionRNBR_BACAM Hydrolyzes phosphodiester bonds in RNA, poly- and oligoribonucleotides resulting in 3'-nucleoside monophosphates via 2',3'-cyclophosphate intermediates.ITR2_ECBEL Inhibits trypsin.ITR2_MOMCO Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Loading citation details.. Citations No citations found See AlsoReferences
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