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]

Subunits

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

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

dimer

Pyrococcus horikoshii

O59179

2 * 25000, dimer of the N-terminal fragment of PH1510 (1510-N, residues 16–236), SDS-PAGE

722647

hexamer

Pyrococcus horikoshii

O59179

molecular modeling of hexameric oligonucleotide binding domains of enzyme C-terminal region of enzyme PH1510 , inter-domain interactions and domain structure, overview

731379

multimer

Pyrococcus horikoshii

O59179

the structure of C-terminal soluble enzyme domain 1510-C, residues 371-441 of PH1510, has a compact five-stranded beta-barrel fold known as an oligosaccharide/oligonucleotide-binding fold (OB-fold). According to crystal packing, 1510-C can assemble into multimers based on a dimer as a basic unit. C-terminal soluble enzyme domain 1510-C also forms a large cylinder-like structure composed of 24 subunits or a large triangular prism-like structure composed of 12 subunits

731822