Evolutionary relationships between heme-binding ferredoxin α + β barrels
نویسندگان
چکیده
منابع مشابه
Helix swapping between two α/β barrels: crystal structure of phosphoenolpyruvate mutase with bound Mg2+–oxalate
Background: Phosphonate compounds are important secondary metabolites in nature and, when linked to macromolecules in eukaryotes, they might play a role in cell signaling. The first obligatory step in the biosynthesis of phosphonates is the formation of a carbon–phosphorus bond by converting phosphoenolpyruvate (PEP) to phosphonopyruvate (P-pyr), a reaction that is catalyzed by PEP mutase. The ...
متن کاملHalf-Barrels Derived from a (β/α)8 Barrel β-Glycosidase Undergo an Activation Process
The evolution of (β/α)8 barrel proteins is currently thought to have involved the fusion of two (β/α)4 half-barrels, thereby conferring stability on the protein structure. After the formation of a whole (β/α)8 barrel, this structure could evolve and diverge to form fully active enzymes. Interestingly, we show here that isolated (β/α)4 half-barrels derived from the N- and C-terminal domains of t...
متن کاملStructural Determinants of Transmembrane β-Barrels.
The recognition of β-barrel membrane proteins based on their sequence is more challenging than the recognition of α-helical membrane proteins. This goal could benefit from a better understanding of the physical determinants of transmembrane β-barrel structure. To that end, we first extend the IMM1 implicit membrane model in a way that allows the modeling of membrane proteins with an internal aq...
متن کاملOn $(α, β)$−Linear Connectivity
In this paper we introduce $(alpha,beta)-$linear connected spaces for nonzero cardinal numbers $alpha$ and $beta$. We show that $(alpha,beta)-$linear connectivity approach is a tool to classify the class of all linear connected spaces.
متن کاملBinding analysis of ferritin with heme using α-casein and biotinylated-hemin: detection of heme-binding capacity of Dpr derived from heme synthesis-deficient Streptococcus mutans.
Bacterial and mammalian ferritins are known to bind heme. The use of α-casein and biotinylated hemin could be applicable to detection of protein-bound heme and of proteins with heme-binding capacity, respectively. Although commercial horse spleen ferritin and purified horse spleen ferritin (L:H subunit ratio=4) bound to an α-casein-coated plate, and this binding could be inhibited by hemin, rec...
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: BMC Bioinformatics
سال: 2016
ISSN: 1471-2105
DOI: 10.1186/s12859-016-1033-6