Literature summary for 3.4.21.105 extracted from

Bondar, A.N.; del Val, C.; White, S.H.
Rhomboid protease dynamics and lipid interactions (2009), Structure, 17, 395-405.

Search for more literature for 3.4.21.105

Application

Application	Comment	Organism
molecular biology	TM5 helix and L1 loop are dynamically coupled so that changes in the dynamics of one are relayed to the other	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
L229V/F232V/W236V	mutation of the TM5 helix leads to a significant enhanced activity. The structures of the TM segments does not change significantly in the triple-Val mutant, but, due to the smaller size of the Val relative to the wild-type residues (Trp, Phe, and Leu), the accessibility of the catalytic Ser from the lateral side increased. This change alone helps explain the enhanced activity of the triple-Val mutant	Escherichia coli
Y138S/F139S/L143S	mutation of the L1 loop leads to a significant reduced activity. The triple-Ser mutation in the L1 loop affects the orientation of the protein within the lipid bilayer and the location of the catalytic Ser	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P09391	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	to derive a dynamic view of GlpG in a fluid lipid bilayer, the lipid interactions of GlpG embedded in 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylcholine (POPE) and 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylethanolamine (POPC) lipid bilayers is examined. The irregular shape and small hydrophobic thickness of the protein cause significant bilayer deformations that may be important for substrate entry into the active site. Hydrogen-bond interactions with lipids are paramount in protein orientation and dynamics. Mutations in the unusual L1 loop cause changes in protein dynamics and protein orientation that are relayed to the His-Ser catalytic dyad. Similarly, mutations in TM5 change the dynamics and structure of the L1 loop	Escherichia coli	?	-	?

Synonyms

Synonyms	Comment	Organism
GlpG	-	Escherichia coli
rhomboid protease	-	Escherichia coli

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Release 2023.1 (January 2023)