3.4.21.B56: Pyrococcus horikoshii membrane protease PH1510

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For detailed information about Pyrococcus horikoshii membrane protease PH1510, go to the full flat file.

Reaction

Synonyms

1510-C, 1510-N, membrane stomatin-specific protease, PH1510, PH1510p, stomatin operon partner protein, Stomatin/STOPP, STOPP, STOPP PH1510

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.21 Serine endopeptidases

                3.4.21.B56 Pyrococcus horikoshii membrane protease PH1510

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Results	in table
1	AA Sequence
2	Cloned(Commentary)
4	Crystallization (Commentary)
4	General Information
12	Inhibitors
6	Localization
1	Molecular Weight [Da]
2	Natural Substrates/ Products (Substrates)
7	Organism
1	pH Optimum
5	Protein Variants
2	Purification (Commentary)
7	Reference
10	Substrates and Products (Substrate)
3	Subunits
16	Synonyms
1	Temperature Optimum [°C]

Crystallization

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Crystallization on EC 3.4.21.B56 - Pyrococcus horikoshii membrane protease PH1510

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

crystal structure of 1510-N (N-terminal region of open reading frame, PH1510 (residues 16–236)) in dimeric form

Pyrococcus horikoshii

O59179

722950

enzyme mutant K138A in complex with a peptide substrate, an enzyme dimer bound to one peptide, X-ray diffraction structure determination and analysis at 2.25 A resolution

Pyrococcus horikoshii

O59179

731295

hanging-drop vapor diffusion method, crystallization of the catalytically inactive mutants S97A and K138A of 1510-N in complex with three kinds of substrate peptides of p-stomatin (234NVIVLMLPME243, 232KSNVIVLML240 and 238LMLPMEMLK246), structural analysis

Pyrococcus horikoshii

O59179

725842

purified recombinant C-terminal soluble domain 1510-C of STOPP PH1510, sitting drop vapor diffusion method, mixing of 0.0005 ml of 5.7 mg/ml protein in 50 mM Tris-HCl, pH 7.5, and 50 mM NaCl with 0.0005 ml of reservoir solution containing 20% v/v Jeffamine M-600 and 0.1 M HEPES-NaOH, pH 7.5, 20°C, X-ray diffraction structure determination and analysis at 2.4 A resolution, molecular replacement, for modelling the structure with PDB ID 2EXD is used method

Pyrococcus horikoshii

O59179

731822