3BPP
1510-N membrane protease K138A mutant specific for a stomatin homolog from Pyrococcus horikoshii
Summary for 3BPP
| Entry DOI | 10.2210/pdb3bpp/pdb |
| Related | 2DEO |
| Descriptor | 1510-N membrane protease (2 entities in total) |
| Functional Keywords | membrane protease, specific for a stomatin homolog, archaea, pyrococcus, thermostable, catalytic dyad, hydrolase |
| Biological source | Pyrococcus horikoshii |
| Total number of polymer chains | 1 |
| Total formula weight | 25368.03 |
| Authors | Yokoyama, H.,Hamamatsu, S.,Fujii, S.,Matsui, I. (deposition date: 2007-12-19, release date: 2008-04-29, Last modification date: 2023-11-01) |
| Primary citation | Yokoyama, H.,Hamamatsu, S.,Fujii, S.,Matsui, I. Novel dimer structure of a membrane-bound protease with a catalytic Ser-Lys dyad and its linkage to stomatin J.SYNCHROTRON RADIAT., 15:254-257, 2008 Cited by PubMed Abstract: 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. PubMed: 18421152DOI: 10.1107/S0909049507068471 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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