Literature summary for 3.4.21.105 extracted from

Zoll, S.; Stanchev, S.; Began, J.; Skerle, J.; Lep?ik, M.; Peclinovska, L.; Majer, P.; Strisovsky, K.
Substrate binding and specificity of rhomboid intramembrane protease revealed by substrate-peptide complex structures (2014), EMBO J., 33, 2408-2421.

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Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with inhibotrs acetyl-L-Ile-L-Ala-L-Thr-L-Ala-chloromethylketone, acetyl-L-Phe-L-Ala-L-Thr-L-Ala-chloromethylketone. Inhibitors bind in a substrate-like manner. The S1 subsite is prominent and merges into the water retention site, suggesting intimate interplay between substrate binding, specificity and catalysis. The S4 subsite is plastically formed by residues of the L1 loop, an important but hitherto enigmatic feature of the rhomboid fold	Escherichia coli

Crystallization (Comment)

Organism

in complex with inhibotrs acetyl-L-Ile-L-Ala-L-Thr-L-Ala-chloromethylketone, acetyl-L-Phe-L-Ala-L-Thr-L-Ala-chloromethylketone. Inhibitors bind in a substrate-like manner. The S1 subsite is prominent and merges into the water retention site, suggesting intimate interplay between substrate binding, specificity and catalysis. The S4 subsite is plastically formed by residues of the L1 loop, an important but hitherto enigmatic feature of the rhomboid fold

Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
acetyl-L-Ile-L-Ala-L-Thr-L-Ala-chloromethylketone	inhibitor derived from the natural rhomboid substrate TatA from bacterium Providencia stuartii, binds in a substrate-like manner	Escherichia coli
acetyl-L-Phe-L-Ala-L-Thr-L-Ala-chloromethylketone	inhibitor derived from the natural rhomboid substrate TatA from bacterium Providencia stuartii, binds in a substrate-like manner	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

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Release 2023.1 (January 2023)