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Literature summary for 3.4.21.B56 extracted from

  • Yokoyama, H.; Takizawa, N.; Kobayashi, D.; Matsui, I.; Fujii, S.
    Crystal structure of a membrane stomatin-specific protease in complex with a substrate peptide (2012), Biochemistry, 51, 3872-3880.
    View publication on PubMed
Search for more literature for 3.4.21.B56

Crystallization (Commentary)

Crystallization (Comment) Organism
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

Protein Variants

Protein Variants Comment Organism
K138A site-directed mutagenesis Pyrococcus horikoshii

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane membrane-bound enzyme Pyrococcus horikoshii 16020
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
p-stomatin PH1511p + H2O Pyrococcus horikoshii the N-terminal region of PH1510p is a serine protease and specifically cleaves the C-terminal hydrophobic region of the p-stomatin PH1511p ?
-
 ?

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii O59179
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information peptide substrate binding structure of the enzyme, detailed analysis and overview. The six central residues, VIVLML, of the peptide are hydrophobic and in a pseudopalindromic structure and therefore favorably fit into the hydrophobic active tunnel of the enzyme dimer, although the enzyme degrades the substrate at only one point. Binding of the substrate causes a large rotational and translational displacement between protomers and produces a tunnel suitable for binding the peptide. When the peptide binds, the flexible L2 loop of one protomer forms beta-strands, whereas that of the other protomer remains in a loop form, indicating that one protomer binds to the peptide more tightly than the other protomer. The Ala138 residues of the two protomers are located very close together, close positioning of the catalytic Ser97 and Lys138 residues may be induced by electrostatic repulsion of the two Lys138 side chains of the protomers Pyrococcus horikoshii ?
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 ?
p-stomatin PH1511p + H2O the N-terminal region of PH1510p is a serine protease and specifically cleaves the C-terminal hydrophobic region of the p-stomatin PH1511p Pyrococcus horikoshii ?
-
 ?

Synonyms

Synonyms Comment Organism
1510-N
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 Pyrococcus horikoshii
membrane stomatin-specific protease
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 Pyrococcus horikoshii
PH1510p
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 Pyrococcus horikoshii

General Information

General Information Comment Organism
additional information the N-terminal region of PH1510p is a serine protease with a catalytic Ser-Lys dyad, Ser97 and Lys138 Pyrococcus horikoshii