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Literature summary for 3.4.21.105 extracted from

  • Zhou, Y.; Moin, S.M.; Urban, S.; Zhang, Y.
    An internal water-retention site in the rhomboid intramembrane protease GlpG ensures catalytic efficiency (2012), Structure, 20, 1255-1263.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular dynamics simulations initiated from both gate-open and gate-closed states of rhomboid GlpG in a phospholipid bilayer. There is rapid loss of crystallographic waters from the active site, but retention of a water cluster within a site formed by His141, Ser181, Ser185, and/or Gln189. Residues Gln189 and Ser185 play an essential role in catalysis with no effect on structural stability Escherichia coli

Protein Variants

Protein Variants Comment Organism
H141F decrease in transition temperature by 6 degrees. Mutant retains almost no activity Escherichia coli
H141T decrease in transition temperature by 11-12 degrees. Mutant retains some activity Escherichia coli
H141V decrease in transition temperature by 11-12 degrees. Mutant retains some activity Escherichia coli
Q189A no catalytic activity, thermostability of mutant is indistinguishable from wild-type Escherichia coli
Q189T no catalytic activity, thermostability of mutant is indistinguishable from wild-type Escherichia coli
S185T mutant retains proteolyitc activity Escherichia coli
S185V transition temperature similar to wild-type, no catalytic activity Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P09391
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
APP-Spi7-Flag + H2O
-
 Escherichia coli ?
-
 ?
Spitz-polyA + H2O
-
 Escherichia coli ?
-
 ?