PDBsum entry 3bpp

Hydrolase

PDB id: 3bpp

Contents

Protein chain

216 a.a. *

Waters ×63

* Residue conservation analysis

PDB id:

3bpp

Name:

Hydrolase

Title:

1510-n membrane protease k138a mutant specific for a stomatin homolog from pyrococcus horikoshii

Structure:

1510-n membrane protease. Chain: a. Fragment: residues 16-236. Synonym: 441aa long hypothetical nfed protein. Engineered: yes. Mutation: yes

Source:

Pyrococcus horikoshii. Organism_taxid: 53953. Gene: ph1510. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.30Å R-factor: 0.244 R-free: 0.310

Authors:

H.Yokoyama,S.Hamamatsu,S.Fujii,I.Matsui

Key ref:

H.Yokoyama et al. (2008). 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. PubMed id: 18421152

Date:

19-Dec-07 Release date: 29-Apr-08

Protein chain

O59179  (STOPP_PYRHO) -  Membrane-bound protease PH1510 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

Seq: 441 a.a.

Struc: 216 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.4.21.- - ?????

J Synchrotron Radiat 15:254-257 (2008)

PubMed id: 18421152

Novel dimer structure of a membrane-bound protease with a catalytic Ser-Lys dyad and its linkage to stomatin.

H.Yokoyama, S.Hamamatsu, S.Fujii, I.Matsui.

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.