Molecular modeling of the HAMP domain of sensory rhodopsin II transducer from Natronomonas pharaonis.

ABSTRACT: The halobacterial transducer of sensory rhodopsin II (HtrII) is a photosignal transducer associated with phototaxis in extreme halophiles. The HAMP domain, a linker domain in HtrII, is considered to play an important role in transferring the signal from the membrane to the cytoplasmic region, although its structure in the complex remains undetermined. To establish the structural basis for understanding the mechanism of signal transduction, we present an atomic model of the structure of the N-terminal HAMP domain from Natronomonas pharaonis (HtrII: 84-136), based on molecular dynamics (MD) simulations. The model was built by homology modeling using the NMR structure of Af1503 from Archaeoglobus fulgidus as a template. The HAMP domains of Af1503 and HtrII were stable during MD

SUBMITTER: Nishikata K 

PROVIDER: S-EPMC5036668 | biostudies-literature | 2010

REPOSITORIES: biostudies-literature