Crystal structure of a supercharged variant of the human enteropeptidase light chain

Peter Simeonov, Michael Zahn, Norbert Sträter*, Thole Zuchner*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

The highly specific serine protease human enteropeptidase light chain cleaves the Asp4Lys recognition sequence and represents an interesting enzyme for biotechnological applications. The human enzyme shows 10 times faster kinetics compared to other animal sources but low solubility under low salt conditions, which hampers protein production and crystallization. Therefore, a supercharged variant (N6D/G21D/G22D/N142D/K210E/C112S) with increased solubility was used for crystallization. The structure (resolution, 1.9 Å) displays a typical α/β trypsin‐like serine protease‐fold. The mutations introduced for protein supercharging generate larger clusters of negative potential on both sites of the active cleft but do not affect the structural integrity of the protein.
Original languageEnglish
Pages (from-to)1907-1910
Number of pages4
JournalProteins: Structure, Function, Bioinformatics
Volume80
Issue number7
Early online date10 Apr 2012
DOIs
Publication statusPublished - 1 Jul 2012

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