نتایج جستجو برای: pbps

تعداد نتایج: 417  

2017
Shubhangi Agarwal Sanjay Dey Biplab Ghosh Maitree Biswas Jhimli Dasgupta

Molecular mechanisms of xenosiderophore and heme acquisitions using periplasmic binding protein (PBP) dependent ATP-binding cassette transporters to scavenge the essential nutrient iron are elusive yet in Vibrio cholerae. Our current study delineates the structures, dynamics and ligand binding properties of two Type III PBPs of V. cholerae, VcFhuD and VcHutB. Through crystal structures and fluo...

Journal: :The Journal of biological chemistry 2004
Audrey Lartigue Arnaud Gruez Loïc Briand Florence Blon Valérie Bézirard Martin Walsh Jean-Claude Pernollet Mariella Tegoni Christian Cambillau

Pheromone binding proteins (PBPs) are small helical proteins ( approximately 13-17 kDa) present in several sensory organs from moth and other insect species. They are involved in the transport of pheromones from the sensillar lymph to the olfactory receptors. We report here the crystal structure of a PBP (Amel-ASP1) originating from the honey-bee (Apis mellifera) antennae and expressed as recom...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2005
Arun V Divakaruni Rachel R Ogorzalek Loo Yongming Xie Joseph A Loo James W Gober

The bacterial actin homolog, MreB, forms helical cables within the cell that are required for maintenance of a rod shape. These helical structures are thought to be involved in the spatial organization of cell wall (peptidoglycan) synthesizing complexes of penicillin-binding proteins (PBPs). Here, we examined the role of the MreC cell shape protein in this process in Caulobacter crescentus. Sub...

Journal: :Journal of bacteriology 1998
T Murray D L Popham P Setlow

Bacillus subtilis strains lacking penicillin-binding protein 1 (PBP1), encoded by ponA, required greater amounts of Mg2+ or Ca2+ for vegetative growth or spore outgrowth than the wild-type strain and strains lacking other high-molecular-weight (HMW) PBPs. Growth of ponA cells in a medium low in Mg2+ also resulted in greatly increased cell bending compared to wild-type cells or cells lacking oth...

Journal: :Journal of the American Chemical Society 2003
Samy O Meroueh George Minasov Wenlin Lee Brian K Shoichet Shahriar Mobashery

Penicillin-binding proteins (PBPs), biosynthetic enzymes of bacterial cell wall assembly, and beta-lactamases, resistance enzymes to beta-lactam antibiotics, are related to each other from an evolutionary point of view. Massova and Mobashery (Antimicrob. Agents Chemother. 1998, 42, 1-17) have proposed that for beta-lactamases to have become effective at their function as antibiotic resistance e...

Journal: :Journal of bacteriology 2015
Anabela de Sousa Borges Jeanine de Keyzer Arnold J M Driessen Dirk-Jan Scheffers

UNLABELLED Membrane proteins need to be properly inserted and folded in the membrane in order to perform a range of activities that are essential for the survival of bacteria. The Sec translocon and the YidC insertase are responsible for the insertion of the majority of proteins into the cytoplasmic membrane. YidC can act in combination with the Sec translocon in the insertion and folding of me...

2016
Bum Han Ryu Tri Duc Ngo Wanki Yoo Sojeong Lee Boo-Young Kim Euijoo Lee Kyeong Kyu Kim T. Doohun Kim

Considering that the prevalence of antibiotic-resistant pathogenic bacteria is largely increasing, a thorough understanding of penicillin-binding proteins (PBPs) is of great importance and crucial significance because this enzyme family is a main target of β-lactam-based antibiotics. In this work, combining biochemical and structural analysis, we present new findings that provide novel insights...

Journal: :Molecular biology and evolution 2003
Kaoru Fukami-Kobayashi Yoshio Tateno Ken Nishikawa

The bacterial LacI/GalR family repressors such as lactose operon repressor (LacI), purine nucleotide synthesis repressor (PurR), and trehalose operon repressor (TreR) consist of not only the N-terminal helix-turn-helix DNA-binding domain but also the C-terminal ligand-binding domain that is structurally homologous to periplasmic sugar-binding proteins. These structural features imply that the r...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2002
Marcus Fehr Wolf B Frommer Sylvie Lalonde

Compartmentation of metabolic reactions and thus transport within and between cells can be understood only if we know subcellular distribution based on nondestructive dynamic monitoring. Currently, methods are not available for in vivo metabolite imaging at cellular or subcellular levels. Limited information derives from methods requiring fixation or fractionation of tissue (1, 2). We thus deve...

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