2IRV

Crystal structure of GlpG, a rhomboid intramembrane serine protease

Summary for 2IRV

• Entry DOI: 10.2210/pdb2irv/pdb
• Related: 2IC8
• Descriptor: Protein glpG, LAURYL DIMETHYLAMINE-N-OXIDE, PHOSPHATE ION, ... (6 entities in total)
• Functional Keywords: membrane protein, cavity, ser-his dyad
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P09391
• Total number of polymer chains: 2
• Total formula weight: 48384.83

Authors

Bibi, E.,Fass, D.,Ben-Shem, A. (deposition date: 2006-10-16, release date: 2006-10-31, Last modification date: 2024-02-21)

Primary citation

Ben-Shem, A.,Fass, D.,Bibi, E.
Structural basis for intramembrane proteolysis by rhomboid serine proteases.
Proc.Natl.Acad.Sci.Usa, 104:462-466, 2007

PubMed Abstract: Intramembrane proteases catalyze peptide bond cleavage of integral membrane protein substrates. This activity is crucial for many biological and pathological processes. Rhomboids are evolutionarily widespread intramembrane serine proteases. Here, we present the 2.3-A-resolution crystal structure of a rhomboid from Escherichia coli. The enzyme has six transmembrane helices, five of which surround a short TM4, which starts deep within the membrane at the catalytic serine residue. Thus, the catalytic serine is in an externally exposed cavity, which provides a hydrophilic environment for proteolysis. Our results reveal a mechanism to enable water-dependent catalysis at the depth of the hydrophobic milieu of the membrane and suggest how substrates gain access to the sequestered rhomboid active site.

PubMed: 17190827
DOI: 10.1073/pnas.0609773104

Experimental method

X-RAY DIFFRACTION (2.3 Å)