نتایج جستجو برای: barrel domain of abompa
تعداد نتایج: 21188282 فیلتر نتایج به سال:
The partially de-N-acetylated poly-β-1,6-N-acetyl-d-glucosamine (dPNAG) polymer serves as an intercellular biofilm adhesin that plays an essential role for the development and maintenance of integrity of biofilms of diverse bacterial species. Translocation of dPNAG across the bacterial outer membrane is mediated by a tetratricopeptide repeat-containing outer membrane protein, PgaA. To understan...
Membrane protein insertion and folding was studied for the major outer membrane protein of Fusobacterium nucleatum (FomA), which is a voltage-dependent general diffusion porin. The transmembrane domain of FomA forms a beta-barrel that is predicted to consist of 14 beta-strands. Here, unfolded FomA is shown to insert and fold spontaneously and quantitatively into phospholipid bilayers upon dilut...
Vibrio cholerae, the enteropathogenic gram negative bacteria is one of the main causative agents of waterborne diseases like cholera. About 1/3(rd) of the organism's genome is uncharacterised with many protein coding genes lacking structure and functional information. These proteins form significant fraction of the genome and are crucial in understanding the organism's complete functional makeu...
Escherichia coli MutY is an adenine and weak guanine DNA glycosylase involved in reducing the mutagenic effects of 7,8-dihydro-8-oxoguanine (GO). MutY contains three structural domains: an iron-sulfur module, a six-helix barrel module with the helix-hairpin-helix motif, and a C-terminal domain. Here, we demonstrate that the mutant MutY(Delta26-134), which lacks the six-helix barrel domain, cann...
Cut out or extrusion of the lag screw from the superior aspect of head and neck of the femur is one of the most common and devastating complications of the surgery of the intertrochanteric fractures with DHS. The exact cause of this complications is unknown, but it seems to be related to osteopenia, inappropriate position of lag screw inside head of the femur and inability of DHS to slide insid...
It has been suggested that protein domains evolved by the non-homologous recombination of building blocks of subdomain size. In earlier work we attempted to recapitulate domain evolution in vitro. We took a polypeptide segment comprising three beta-strands in the monomeric, five-stranded beta-barrel cold shock protein (CspA) of Escherichia coli as a building block. This segment corresponds to a...
The FhuA outer membrane protein of Escherichia coli actively transports ferrichrome, albomycin, and rifamycin CGP 4832, and confers sensitivity to microcin J25, colicin M, and the phages T1, T5, and phi80. Guided by the FhuA crystal structure and derived predictions on how FhuA might function, mutants were isolated in the cork domain (residues 1 to 160) and in the beta-barrel domain (residues 1...
Barrels are patterned groups of neurons in rodent somatosensory cortex that correspond one to one with the animal's facial whiskers. Dirichlet domains are a class of convex polygon found frequently in nature, often arising by nucleation from center points. Analytic and graphical methods were devised to verify the hypothesis that Dirichlet domains accurately describe the adult barrel fields of n...
This work presents a simulation approach to the design and economic evaluation of fuel oil hydrotreating processes for the control of SO2 and NOx emission in an Iranian steam power plant. The percent of fuel oil desulphurization was estimated from the SO2 emissions standards for power plants. Based on two different scenarios according to (I) European and (II) Iranian standards, the design and s...
Lysine 5,6-aminomutase is an adenosylcobalamin and pyridoxal-5'-phosphate-dependent enzyme that catalyzes a 1,2 rearrangement of the terminal amino group of dl-lysine and of l-beta-lysine. We have solved the x-ray structure of a substrate-free form of lysine-5,6-aminomutase from Clostridium sticklandii. In this structure, a Rossmann domain covalently binds pyridoxal-5'-phosphate by means of lys...
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