4DGJ

Structure of a human enteropeptidase light chain variant

Summary for 4DGJ

Entry DOI	10.2210/pdb4dgj/pdb
Related	1EKB
Descriptor	Enteropeptidase catalytic light chain (2 entities in total)
Functional Keywords	serine protease, hydrolase
Biological source	Homo sapiens (human)
Total number of polymer chains	4
Total formula weight	105518.69
Authors	Zahn, M.,Simeonov, P.,Straeter, N. (deposition date: 2012-01-26, release date: 2012-04-18, Last modification date: 2024-11-27)
Primary citation	Simeonov, P.,Zahn, M.,Strater, N.,Zuchner, T. Crystal structure of a supercharged variant of the human enteropeptidase light chain. Proteins, 80:1907-1910, 2012 Cited by PubMed 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. PubMed: 22488687 DOI: 10.1002/prot.24084 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.9 Å)

Structure validation