Novel dimer structure of a membrane-bound protease with a catalytic Ser-Lys dyad and its linkage to stomatin
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 t...
| Veröffentlicht in: | Journal of synchrotron radiation. - 1994. - 15(2008), Pt 3 vom: 07. Mai, Seite 254-7 |
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| Weitere Verfasser: | , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2008
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| Zugriff auf das übergeordnete Werk: | Journal of synchrotron radiation |
| Schlagworte: | Journal Article Archaeal Proteins Membrane Proteins Serine 452VLY9402 Serine Endopeptidases EC 3.4.21.- Lysine K3Z4F929H6 |
| Zusammenfassung: | 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 |
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| Beschreibung: | Date Completed 31.07.2008 Date Revised 08.04.2024 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1600-5775 |
| DOI: | 10.1107/S0909049507068471 |