Crystal structure of a photoactive yellow protein from a sensor histidine kinase : Conformational variability and signal transduction
نویسندگان
چکیده
MEDICAL SCIENCES. For the article ‘‘Linkage disequilibrium in human populations,’’ by Christine Lonjou, Weihua Zhang, Andrew Collins, William J. Tapper, Eiram Elahi, Nikolas Maniatis, and Newton E. Morton, which appeared in issue 10, May 13, 2003, of Proc. Natl. Acad. Sci. USA (100, 6069–6074; First Published April 29, 2003; 10.1073 pnas.1031521100), due to a printer’s error, the last three column headings in Table 5 incorrectly contained dashes in ‘‘European-Asian,’’ ‘‘AfricanAmerican-Yoruban,’’ and ‘‘African-Eurasian’’ instead of the necessary minus signs. The corrected table appears below.
منابع مشابه
Crystal structure of a photoactive yellow protein from a sensor histidine kinase: conformational variability and signal transduction.
Photoactive yellow protein (E-PYP) is a blue light photoreceptor, implicated in a negative phototactic response in Ectothiorhodospira halophila, that also serves as a model for the Per-Arnt-Sim superfamily of signaling molecules. Because no biological signaling partner for E-PYP has been identified, it has not been possible to correlate any of its photocycle intermediates with a relevant signal...
متن کاملاثر فلاونوئید کوئرستین بر تغییرات ساختاری ناحیه کینازی پروتئین نوترکیب FGFR2b
Background and Aim: Antioxidants are compounds that protect cells from attacks of free radicals. Lack of balance between antioxidants and free radicals results in oxidative stress, which ultimately results in cell damage. The effects of flavonoids are not related solely to their antioxidant properties, but also to their effects on cellular signal pathways. The present study was conducted to eva...
متن کاملCrystal structure of Pseudomonas aeruginosa bacteriophytochrome: photoconversion and signal transduction.
Phytochromes are red-light photoreceptors that regulate light responses in plants, fungi, and bacteria via reversible photoconversion between red (Pr) and far-red (Pfr) light-absorbing states. Here we report the crystal structure at 2.9 A resolution of a bacteriophytochrome from Pseudomonas aeruginosa with an intact, fully photoactive photosensory core domain in its dark-adapted Pfr state. This...
متن کاملStructural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis.
Signal transduction proteins such as bacterial sensor histidine kinases, designed to transition between multiple conformations, are often ruled by unstable transient interactions making structural characterization of all functional states difficult. This study explored the inactive and signal-activated conformational states of the two catalytic domains of sensor histidine kinases, HisKA and HAT...
متن کاملStructure of a biological oxygen sensor: a new mechanism for heme-driven signal transduction.
The FixL proteins are biological oxygen sensors that restrict the expression of specific genes to hypoxic conditions. FixL's oxygen-detecting domain is a heme binding region that controls the activity of an attached histidine kinase. The FixL switch is regulated by binding of oxygen and other strong-field ligands. In the absence of bound ligand, the heme domain permits kinase activity. In the p...
متن کامل