Rv0216, a conserved hypothetical protein fromMycobacterium tuberculosisthat is essential for bacterial survival during infection, has a double hotdog fold
نویسندگان
چکیده
منابع مشابه
Rv0216, a conserved hypothetical protein from Mycobacterium tuberculosis that is essential for bacterial survival during infection, has a double hotdog fold.
The Mycobacterium tuberculosis genome contains about 4000 genes, of which approximately a third code for proteins of unknown function or are classified as conserved hypothetical proteins. We have determined the three-dimensional structure of one of these, the rv0216 gene product, which has been shown to be essential for M. tuberculosis growth in vivo. The structure exhibits the greatest similar...
متن کاملBicaudal Is a Conserved Substrate for Drosophila and Mammalian Caspases and Is Essential for Cell Survival
Members of the caspase family of cysteine proteases coordinate cell death through restricted proteolysis of diverse protein substrates and play a conserved role in apoptosis from nematodes to man. However, while numerous substrates for the mammalian cell death-associated caspases have now been described, few caspase substrates have been identified in other organisms. Here, we have utilized a pr...
متن کاملA Ca2+-dependent bacterial antifreeze protein domain has a novel beta-helical ice-binding fold.
AFPs (antifreeze proteins) are produced by many organisms that inhabit ice-laden environments. They facilitate survival at sub-zero temperatures by binding to, and inhibiting, the growth of ice crystals in solution. The Antarctic bacterium Marinomonas primoryensis produces an exceptionally large(>1 MDa) hyperactive Ca2+-dependent AFP. We have cloned,expressed and characterized a 322-amino-acid ...
متن کاملA Ca2+-dependent bacterial antifreeze protein domain has a novel β-helical ice-binding fold
AFPs (antifreeze proteins) are produced by many organisms that inhabit ice-laden environments. They facilitate survival at sub-zero temperatures by binding to, and inhibiting, the growth of ice crystals in solution. The Antarctic bacterium Marinomonas primoryensis produces an exceptionally large (>1 MDa) hyperactive Ca2+-dependent AFP. We have cloned, expressed and characterized a 322-amino-aci...
متن کاملNeisseria conserved hypothetical protein DMP12 is a DNA mimic that binds to histone-like HU protein
DNA mimic proteins are unique factors that control the DNA-binding activity of target proteins by directly occupying their DNA-binding sites. To date, only a few DNA mimic proteins have been reported and their functions analyzed. Here, we present evidence that the Neisseria conserved hypothetical protein DMP12 should be added to this list. Our gel filtration and analytical ultracentrifugation r...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Protein Science
سال: 2005
ISSN: 0961-8368,1469-896X
DOI: 10.1110/ps.051442305