2C4B

Inhibitor cystine knot protein McoEeTI fused to the catalytically inactive barnase mutant H102A

Summary for 2C4B

• Entry DOI: 10.2210/pdb2c4b/pdb
• Descriptor: BARNASE MCOEETI FUSION, NONAETHYLENE GLYCOL, GLYCEROL, ... (9 entities in total)
• Functional Keywords: squash inhibitor, hybrid microprotein, fusion protein, ribonuclease, endonuclease, hydrolase, nuclease, protease inhibitor, serine protease inhibitor
• Biological source: BACILLUS AMYLOLIQUEFACIENS; More
• Total number of polymer chains: 2
• Total formula weight: 35792.51

Authors

Niemann, H.H.,Schmoldt, H.U.,Wentzel, A.,Kolmar, H.,Heinz, D.W. (deposition date: 2005-10-18, release date: 2005-11-21, Last modification date: 2024-10-23)

Primary citation

Niemann, H.H.,Schmoldt, H.U.,Wentzel, A.,Kolmar, H.,Heinz, D.W.
Barnase Fusion as a Tool to Determine the Crystal Structure of the Small Disulfide-Rich Protein Mcoeeti.
J.Mol.Biol., 356:1-, 2006

PubMed Abstract: 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.

PubMed: 16337652
DOI: 10.1016/J.JMB.2005.11.005

Experimental method

X-RAY DIFFRACTION (1.3 Å)