Characterization of a conserved α-helical, coiled-coil motif at the C-terminal domain of the ATP-dependent FtsH (HflB) protease of Escherichia coli 1 1Edited by J. Karn

2000 ◽  
Vol 299 (4) ◽  
pp. 953-964 ◽  
Author(s):  
Yoram Shotland ◽  
Dinah Teff ◽  
Simi Koby ◽  
Oren Kobiler ◽  
Amos B Oppenheim
Keyword(s):  
Escherichia Coli ◽  
Coiled Coil ◽  
Terminal Domain

scholarly journals Characterization of Two New Aminopeptidases in Escherichia coli

2005 ◽  
Vol 187 (11) ◽  
pp. 3671-3677 ◽  
Author(s):  
Yu Zheng ◽  
Richard J. Roberts ◽  
Simon Kasif ◽  
Chudi Guan
Keyword(s):  
Escherichia Coli ◽  
Stop Codon ◽  
Bacterial Species ◽  
Start Codon ◽  
Aminopeptidase Activity ◽  
Peptide Substrates ◽  
E Coli ◽  
Terminal Domain ◽  
Methionyl Aminopeptidase

ABSTRACT Two genes in the Escherichia coli genome, ypdE and ypdF, have been cloned and expressed, and their products have been purified. YpdF is shown to be a metalloenzyme with Xaa-Pro aminopeptidase activity and limited methionine aminopeptidase activity. Genes homologous to ypdF are widely distributed in bacterial species. The unique feature in the sequences of the products of these genes is a conserved C-terminal domain and a variable N-terminal domain. Full or partial deletion of the N terminus in YpdF leads to the loss of enzymatic activity. The conserved C-terminal domain is homologous to that of the methionyl aminopeptidase (encoded by map) in E. coli. However, YpdF and Map differ in their preference for the amino acid next to the initial methionine in the peptide substrates. The implication of this difference is discussed. ypdE is the immediate downstream gene of ypdF, and its start codon overlaps with the stop codon of ypdF by 1 base. YpdE is shown to be a metalloaminopeptidase and has a broad exoaminopeptidase activity.

scholarly journals Biophysical and functional characterization of the N-terminal domain of the cat T1R1 umami taste receptor expressed in Escherichia coli

PLoS ONE ◽  
2017 ◽  
Vol 12 (10) ◽  
pp. e0187051 ◽  
Author(s):  
Christine Belloir ◽  
Jimmy Savistchenko ◽  
Fabrice Neiers ◽  
Andrew J. Taylor ◽  
Scott McGrane ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Functional Characterization ◽  
Taste Receptor ◽  
Umami Taste ◽  
Terminal Domain

scholarly journals Isolation and characterization of the flavin-binding domain of flavocytochrome b2 expressed independently in Escherichia coli

1995 ◽  
Vol 309 (2) ◽  
pp. 601-605 ◽  
Author(s):  
A Balme ◽  
C E Brunt ◽  
R L Pallister ◽  
S K Chapman ◽  
G A Reid
Keyword(s):  
Escherichia Coli ◽  
Binding Domain ◽  
Flavin Mononucleotide ◽  
Exponential Process ◽  
Flavocytochrome B2 ◽  
Terminal Domain ◽  
Isolation And Characterization ◽  
Flavin Binding ◽  
Single Exponential

Flavocytochrome b2 consists of two distinct domains. The N-terminal domain contains protohaem IX and the larger, C-terminal domain contains flavin mononucleotide (FMN). We describe here the isolation of the flavin-binding domain expressed in Escherichia coli independent of the cytochrome domain. The isolated domain is an efficient lactate dehydrogenase with ferricyanide as electron acceptor but reduces cytochrome c, the physiological oxidant for flavocytochrome b2, extremely poorly; electron transfer from the flavin-binding domain to the separately expressed cytochrome domain is undetectable. FMN reduction by lactate occurs as a single exponential process in the isolated flavin-binding domain, in contrast to the biphasic kinetics observed with native flavocytochrome b2.

scholarly journals Novel view of the architecture of the non-catalytic n-terminal region of ATP-dependent lona proteases

2010 ◽  
Vol 56 (3) ◽  
pp. 412-419
Author(s):  
T.V. Rotanova ◽  
E.E. Melnikov
Keyword(s):  
Escherichia Coli ◽  
Quality Control ◽  
Protein Quality ◽  
Coiled Coil ◽  
Terminal Region ◽  
Intracellular Location ◽  
Terminal Domain ◽  
And Topology ◽  
Lon Proteases ◽  
Protein Quality Control System

ATP-Dependent Lon proteases are components of the protein quality control system, which maintains a keeping of cellular proteome. Lon family consists of two subfamilies A and B, differing in subunit architecture and intracellular location. The reinterpretation of the domain organization of the non-catalytic N-terminal region of ATP-dependent LonA proteases is proposed. Using Escherichia coli LonA protease (EcLon) as an example it has been shown that a fragment (αN-domain), which is located between the N-terminal domain and the ААА+ module of that protein, is similar to the α1-domain of the first ААА+ module of chaperone-disaggregase ClpB. A coiled-coil (СС) region included in the αN-domain of LonA is similar to the M domain of ClpB chaperones, which is inserted into the α1-domain. This region is suggested to adopt the structure similar to the propeller-like (PL) domain. The typical architecture of the N-terminal region of LonA proteases is postulated to be characterized by the obligatory presence of a PL domain, included in the αN-domain, but may vary in the length and topology of the preceding N-terminal domain.

scholarly journals The Symmetrical Structure of Structural Maintenance of Chromosomes (SMC) and MukB Proteins: Long, Antiparallel Coiled Coils, Folded at a Flexible Hinge

1998 ◽  
Vol 142 (6) ◽  
pp. 1595-1604 ◽  
Author(s):  
Thomas E. Melby ◽  
Charles N. Ciampaglio ◽  
Gina Briscoe ◽  
Harold P. Erickson
Keyword(s):  
Escherichia Coli ◽  
Coiled Coil ◽  
Biomechanical Properties ◽  
Coiled Coils ◽  
Symmetrical Structure ◽  
Terminal Domain ◽  
Symmetrical Molecule ◽  
Almost All ◽  
Structural Maintenance Of Chromosomes ◽  
Smc Proteins

Structural maintenance of chromosomes (SMC) proteins function in chromosome condensation and several other aspects of DNA processing. They are large proteins characterized by an NH2-terminal nucleotide triphosphate (NTP)-binding domain, two long segments of coiled coil separated by a hinge, and a COOH-terminal domain. Here, we have visualized by EM the SMC protein from Bacillus subtilis (BsSMC) and MukB from Escherichia coli, which we argue is a divergent SMC protein. Both BsSMC and MukB show two thin rods with globular domains at the ends emerging from the hinge. The hinge appears to be quite flexible: the arms can open up to 180°, separating the terminal domains by 100 nm, or close to near 0°, bringing the terminal globular domains together. A surprising observation is that the ∼300–amino acid–long coiled coils are in an antiparallel arrangement. Known coiled coils are almost all parallel, and the longest antiparallel coiled coils known previously are 35–45 amino acids long. This antiparallel arrangement produces a symmetrical molecule with both an NH2- and a COOH-terminal domain at each end. The SMC molecule therefore has two complete and identical functional domains at the ends of the long arms. The bifunctional symmetry and a possible scissoring action at the hinge should provide unique biomechanical properties to the SMC proteins.

scholarly journals The Escherichia coli cellulose synthase subunit G (BcsG) is a Zn2+-dependent phosphoethanolamine transferase

2020 ◽  
Vol 295 (18) ◽  
pp. 6225-6235 ◽  
Author(s):  
Alexander C. Anderson ◽  
Alysha J. N. Burnett ◽  
Lana Hiscock ◽  
Kenneth E. Maly ◽  
Joel T. Weadge
Keyword(s):  
Escherichia Coli ◽  
Catalytic Mechanism ◽  
Cellulose Synthase ◽  
Gram Negative Bacteria ◽  
Membrane Phospholipids ◽  
Colistin Resistance ◽  
E Coli ◽  
Terminal Domain

Bacterial biofilms are cellular communities that produce an adherent matrix. Exopolysaccharides are key structural components of this matrix and are required for the assembly and architecture of biofilms produced by a wide variety of microorganisms. The human bacterial pathogens Escherichia coli and Salmonella enterica produce a biofilm matrix composed primarily of the exopolysaccharide phosphoethanolamine (pEtN) cellulose. Once thought to be composed of only underivatized cellulose, the pEtN modification present in these matrices has been implicated in the overall architecture and integrity of the biofilm. However, an understanding of the mechanism underlying pEtN derivatization of the cellulose exopolysaccharide remains elusive. The bacterial cellulose synthase subunit G (BcsG) is a predicted inner membrane–localized metalloenzyme that has been proposed to catalyze the transfer of the pEtN group from membrane phospholipids to cellulose. Here we present evidence that the C-terminal domain of BcsG from E. coli (EcBcsGΔN) functions as a phosphoethanolamine transferase in vitro with substrate preference for cellulosic materials. Structural characterization of EcBcsGΔN revealed that it belongs to the alkaline phosphatase superfamily, contains a Zn2+ ion at its active center, and is structurally similar to characterized enzymes that confer colistin resistance in Gram-negative bacteria. Informed by our structural studies, we present a functional complementation experiment in E. coli AR3110, indicating that the activity of the BcsG C-terminal domain is essential for integrity of the pellicular biofilm. Furthermore, our results established a similar but distinct active-site architecture and catalytic mechanism shared between BcsG and the colistin resistance enzymes.

scholarly journals Mapping the MinE Site Involved in Interaction with the MinD Division Site Selection Protein of Escherichia coli

2003 ◽  
Vol 185 (16) ◽  
pp. 4948-4955 ◽  
Author(s):  
Lu-Yan Ma ◽  
Glenn King ◽  
Lawrence Rothfield
Keyword(s):  
Escherichia Coli ◽  
Coiled Coil ◽  
Yeast Two Hybrid ◽  
Terminal Domain ◽  
Division Site ◽  
Coil Structure ◽  
Extended Surface ◽  
The Mind ◽  
Two Hybrid ◽  
Helical Region

ABSTRACT Interactions between the MinD and MinE proteins are required for proper placement of the Escherichia coli division septum. The site within MinE that is required for interaction with MinD was mapped by studying the effects of site-directed minE mutations on MinD-MinE interactions in yeast two-hybrid and three-hybrid experiments. This confirmed that the MinE N-terminal domain is responsible for the interaction of MinE with MinD. Mutations that interfered with the interaction defined an extended surface on one face of the α-helical region of the MinE N-terminal domain, consistent with the idea that the MinE-MinD interaction involves formation of a coiled-coil structure by interaction with a complementary helical surface within MinD.

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