The role of L1 loop in the mechanism of rhomboid intramembrane protease GlpG.

doi:10.1016/j.jmb.2007.10.014

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

The role of L1 loop in the mechanism of rhomboid intramembrane protease GlpG.

Journal of molecular biology - 7 Dec 2007

Wang Yongcheng, Maegawa Saki, Akiyama Yoshinori, Ha Ya

Abstract excerpt

Intramembrane proteases are important enzymes in biology. The recently solved crystal structures of rhomboid protease GlpG have provided useful insights into the mechanism of these membrane proteins. Besides revealing an internal water-filled cavity that harbored the Ser-His catalytic dyad, the crystal structure identified a novel structural domain (L1 loop) that lies on the side of the transmembrane helices....

Topics

Amino Acid Sequence
Cell Membrane
DNA-Binding Proteins
Endopeptidases
Escherichia coli Proteins
Hydrophobic and Hydrophilic Interactions
Membrane Proteins
Models, Molecular
Molecular Sequence Data
Mutation
Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 17976648
DOI: 10.1016/j.jmb.2007.10.014
PMCID: PMC2128867

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics