3bpp
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Revision as of 10:33, 30 April 2008
1510-N membrane protease K138A mutant specific for a stomatin homolog from Pyrococcus horikoshii
Overview
Membrane-bound proteases are involved in various regulatory functions. A previous report indicates that the N-terminal region of PH1510 (1510-N) from the hyperthermophilic archaeon Pyrococcus horikoshii is a serine protease with a catalytic Ser-Lys dyad (Ser97 and Lys138), and specifically cleaves the C-terminal hydrophobic region of the p-stomatin PH1511. According to the crystal structure of the wild-type 1510-N in dimeric form, the active site around Ser97 is in a hydrophobic environment suitable for the hydrophobic substrates. This article reports the crystal structure of the K138A mutant of 1510-N at 2.3 A resolution. The determined structure contains one molecule per asymmetric unit, but 1510-N is active in dimeric form. Two possible sets of dimer were found from the symmetry-related molecules. One dimer is almost the same as the wild-type 1510-N. Another dimer is probably in an inactive form. The L2 loop, which is disordered in the wild-type structure, is significantly kinked at around A-138 in the K138A mutant. Thus Lys138 probably has an important role on the conformation of L2.
About this Structure
3BPP is a Single protein structure of sequence from Pyrococcus horikoshii. Full crystallographic information is available from OCA.
Reference
Novel dimer structure of a membrane-bound protease with a catalytic Ser-Lys dyad and its linkage to stomatin., Yokoyama H, Hamamatsu S, Fujii S, Matsui I, J Synchrotron Radiat. 2008 May;15(Pt 3):254-7. Epub 2008 Apr 18. PMID:18421152 Page seeded by OCA on Wed Apr 30 13:33:01 2008
