Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4HDD

Domain swapping in the cytoplasmic domain of the Escherichia coli rhomboid protease

Summary for 4HDD
Entry DOI10.2210/pdb4hdd/pdb
Related2lep
DescriptorRhomboid protease GlpG, ACETATE ION (3 entities in total)
Functional Keywordsdomain swapping, peptidase, rhomboid protease, intramembrane protease, membrane, hydrolase
Biological sourceEscherichia coli
Cellular locationCell inner membrane; Multi-pass membrane protein: P09391
Total number of polymer chains1
Total formula weight9171.84
Authors
Lazareno-Saez, C.,Arutyunova, E.,Coquelle, N.,Lemieux, M.J. (deposition date: 2012-10-02, release date: 2013-02-06, Last modification date: 2024-10-30)
Primary citationLazareno-Saez, C.,Arutyunova, E.,Coquelle, N.,Lemieux, M.J.
Domain swapping in the cytoplasmic domain of the Escherichia coli rhomboid protease.
J.Mol.Biol., 425:1127-1142, 2013
Cited by
PubMed Abstract: Rhomboids are membrane-embedded serine proteases that cleave membrane protein substrates. Escherichia coli rhomboid GlpG (ecGlpG) consists of an N-terminal cytoplasmic domain and a membrane domain containing the active site. We determined the crystal structure of the soluble cytoplasmic domain of ecGlpG at 1.35Å resolution and examined whether this domain affected the catalytic activity of the enzyme. The structure revealed that the ecGlpG cytoplasmic domain exists as a dimer with extensive domain swapping between the two monomers. Domain-swapped dimers can be isolated from the full-length protein, suggesting that this is a physiologically relevant structure. An extensive steady-state kinetic analysis of the full-length ecGlpG and its membrane domain using soluble and transmembrane model protein substrates resulted in an unexpected conclusion: removal of the cytoplasmic domain does not alter the catalytic parameters for detergent-solubilized rhomboid for both substrates.
PubMed: 23353827
DOI: 10.1016/j.jmb.2013.01.019
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.35 Å)
Structure validation

243531

数据于2025-10-22公开中

PDB statisticsPDBj update infoContact PDBjnumon