Literature summary for 3.4.21.105 extracted from

Reddy, T.; Rainey, J.K.
Multifaceted substrate capture scheme of a rhomboid protease (2012), J. Phys. Chem. B, 116, 8942-8954.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
Coarse-grained molecular dynamics simulations in hydrated lipid bilayers to study the interaction of rhomboid protease GlpG with the transmembrane domain of the substrate Spitz. Spitz does not associate with GlpG exclusively at the putative substrate gate near TMD 5. Instead, there are six prominent and stable interaction sites, including one between TMDs 1 and 3, with the closest enzyme-substrate proximity occurring at the ends of helical transmembrane domains or in loops. The initial interaction between enzyme and substrate is not limited to a single site on the enzyme, and may be driven by juxtamembrane electrostatic interactions	Escherichia coli

Crystallization (Comment)

Organism

Coarse-grained molecular dynamics simulations in hydrated lipid bilayers to study the interaction of rhomboid protease GlpG with the transmembrane domain of the substrate Spitz. Spitz does not associate with GlpG exclusively at the putative substrate gate near TMD 5. Instead, there are six prominent and stable interaction sites, including one between TMDs 1 and 3, with the closest enzyme-substrate proximity occurring at the ends of helical transmembrane domains or in loops. The initial interaction between enzyme and substrate is not limited to a single site on the enzyme, and may be driven by juxtamembrane electrostatic interactions

Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
beta-lactamase Spitz transmembrane domain + H2O	34 residue peptide, sequence KRPRPMLEKASIASGAMCALVFMLFVCLAFYLRK	Escherichia coli	?	-	?

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Release 2023.1 (January 2023)