Rhomboid Protease Dynamics and Lipid Interactions
Metadatos
Mostrar el registro completo del ítemEditorial
Elsevier
Materia
Inteligencia artificial Artificial intelligence
Fecha
2009-03-11Referencia bibliográfica
Ana-Nicoleta Bondar, Coral del Val, Stephen H. White, Rhomboid Protease Dynamics and Lipid Interactions, Structure, Volume 17, Issue 3, 2009, Pages 395-405, ISSN 0969-2126, [https://doi.org/10.1016/j.str.2008.12.017]
Patrocinador
National Institute of General Medical Sciences (GM-74637)Resumen
Intramembrane proteases, which cleave transmembrane
(TM) helices, participate in numerous biological
processes encompassing all branches of life.
Several crystallographic structures of Escherichia
coli GlpG rhomboid protease have been determined.
In order to understand GlpG dynamics and lipid interactions
in a native-like environment, we have examined
the molecular dynamics of wild-type and mutant
GlpG in different membrane environments. The irregular
shape and small hydrophobic thickness of the
protein cause significant bilayer deformations that
may be important for substrate entry into the active
site. Hydrogen-bond interactions with lipids are
paramount in protein orientation and dynamics.
Mutations in the unusual L1 loop cause changes in
protein dynamics and protein orientation that are
relayed to the His-Ser catalytic dyad. Similarly,mutations
in TM5 change the dynamics and structure of
the L1 loop. These results imply that the L1 loop
has an important regulatory role in proteolysis.