Escherichia coli primary structure

M.E. Schinia, L. Maffey, D. Barra, F. Bossa, K. Puget, and A.M. Michelson, The primary structure of iron superoxide dismutase from Escherichia coli. FEBS Lett. 221, 87-90 (1987). 

Anderson, J. P., Cappello.J., and Martin, D. C. (1994). Morphology and primary crystal-structure of a silk-like protein polymer synthesized by genetically-engineered Escherichia-coli bacteria. Biopolymers 34, 1049-1058. 

Appendix Primary Structure of Escherichia coli Ribosomal Proteins... 

Gordon, D. M., Bauer, S., and Johnson, J. R. (2002). The genetic structure of Escherichia coli populations in primary and secondary habitats. Microbiology 148, 1513-1522. 

Comeau, D.E. Ikenaka, K. Tsung, K.L. Inouye, M. Primary characterization of the protein products of the Escherichia coli ompB locus structure and regulation of synthesis of the OmpR and EnvZ proteins. J. Bacteriol., 164, 578-584 (1985)... 

Fujita, N., Miwa, T., Ishijima, S., Izui, K. Katsuki, H. (1984). The primary structure of phosphoeno/pyruvate carboxylase of Escherichia coli. Nucleotide sequence of the ppc gene and deduced amino acid sequence. Journal of Biochemistry 95, 909-16. 

T. Malta and G. Matsuda. The primary structure of l-aspaiaginase from Escherichia coli. Hoppe Seyter s Z PfiystoL Chem. 361 105 (1980). 

Takahashi et al.61s further identified the primary structure by preparing a cDNA library from A. fumigatus induced with fructosylpropylamine and isolated a clone using a polyclonal Amadoriase II antibody. The structure comprised 438 amino acid residues, corresponding to 48.798 kDa. The identity of the Amadoriase n cDNA was further confirmed by expression in Escherichia coli cells with an inducible expression system. Northern-blotting analysis showed that Amadoriase II was induced by fructosylpropylamine in a dose-dependent manner. The sequence determined showed the enzyme to represent a new family of mammalian enzymes. The sequence exhibited 82 and 36% identity and 92 and 65% similarity, respectively, with the two sequences determined by Yoshida et al.616 Amadori products have been implicated in the formation of H202, but the in vivo mechanism needs to be elucidated further. 

The term quaternary structure was proposed to supplement the terms primary, secondary, and tertiary structure, 9 and refers to the spatial arrangement of noncovalently linked polypeptides which we shall call subunits. Generally, a subunit is defined as a tertiary structural unit composed of a single polypeptide, but the definition is somewhat ambiguous. In aspartate transcarbamoylase from Escherichia coli, for example, tertiary structural units composed of three catalytic polypeptide chains are called catalytic subunits and those composed of two regulatory chains are called regulatory subunits.2)... 

Fig. 5.1 Primary structures of AspATs from various species. P, C, H, Hu, R and M denote for pig, chicken, hamster, human, rat and mouse, respectively, c and m stand for cytosolic and mitochondrial, respectively. eAspAT and tAspAT denote Escherichia coli AspAT and Thermostable AspAT from Thermophilic Bacilus species19 , respectively. Letters in bold face type represent residues discussed in the text.

Although their primary structures seem quite similar RNA and DNA are really veryt different polymers. The molar mass of DNA is considerably higher often being in the hundreds of millions. The molar mass of DNA in the bacterium Escherichia coli is some 2.5 x 109 (Stevens 1999). If the polymer were stretched out, it would be several millimeters long. To fit into a cell nucleus approximately 5 micrometers in diameter the DNA molecule must be extensively folded. 

CZE has been utilized to determine the absence of hGh variants in various preparations. Isoforms resulting from primary structure cleavage, monodeamidation at two different positions, amino terminal succinylation, and a HIS to GLN replacement have been found at position 18 in hGH produced by Escherichia coli.iS,i9 The separations have been achieved in uncoated capillaries with 100 m M phosphate buffer (pH 6.0). 

Baecker, P. A., Greenberg, E., and Preiss, J. 1986. Biosynthesis of bacterial glycogen Primary structure of Escherichia coli 1,4-a-D-glucan 1,4-a-D-glucan 6-a-D-(glucano)-transferase as deduced from the nucleotide sequence of the glgB gene. J. Biol. Chem. 261,8738-8743. 

The production of molecular hydrogen was measured in the effluent gas of seven fermentations [58]. The aim of this primary investigation was to study the use of a H2-sensitive metal-oxide-semiconductor structure in physiological studies of Escherichia coli. In order to yield more information, the metabolic heat was measured with a flow micro calorimeter in parallel with the determination of molecular hydrogen. 

Borodovskii M., Sprizhitskii Yu., Golovanov E., Alexandrov N. (1986) Statistical patterns in the primary structures of functional regions of the genome in Escherichia coli. II. Nonuniform Markov Models. Molekulyarnaya Biologia, 20, 1114-1123. 

In the amine oxidase from Escherichia coli, the topa quinone was confirmed by a detailed analysis of the cofactor dipeptide X-Asp [67] and the resonance Raman spectrometry of the enzyme and its derivatives[68,69]. The primary structure of the enzyme also contains the cofactor consensus sequence [70]. More bacterial genes were shown to encode proteins containing the topa quinone consensus sequence, such as amine oxidase from Klebsiella aerogenes [71], phenethylamine oxidase and histamine oxidase from Arthrobacter globiformis [72,73], and methylamine oxidase from Arthrobacter strain PI [74]. Amino acid sequences around the position of the cofactor for selected amine oxidases from various sources are given in Table 1. 

Comparison of the molecular size of native enzymes estimated by gel filtration and that of purified enzymes on SDS-PAGE indicates that native enzymes of winter squash [59] and zucchini [67] are present in a dimeric form, whereas those of tomato [51] and apple fruits [61] are in a monomers. However, Satoh et al. [68] reported that ACC synthases expressed in Escherichia coli transformed with cDNAs for tomato enzymes (LE-ACS2 and LE-ACS4) were present as dimers as were the winter squash enzymes similarly expressed in E. coli from two different cDNAs [CMW33 (CM-ACSl) and CMAlOl (CM-ACS2)]. It is possible that although, in its primary structure ACC synthase tends to dimerize, tomato ACC synthase is so modified after translation in vivo that dimerization is prevented. The exact nature of the modification is not known. Li and Mattoo [69] reported that dimerization of tomato enzyme expressed in E. coli was prevented when the 52 amino acid residues at the carboxyl terminal were deleted. 

The cDNA and corresponding primary amino acid sequences of several CPRs including rat , rabbit- , and human were obtained by the mid-1980s, and the development of Escherichia coli expression systems paved the way for detailed molecular characterization of the polypeptide through site-directed mutagenesis. The three-dimensional structure of rat CPR was determined by X-ray crystallography in 1997 by Kim and coworkers -, providing the structural prototype for dual flavin oxidoreductases. 

Figure 6.16 Electron Density Map Example of an electron density map generated computationally from electron density data that has been derived by the application of the equations and principles described in the main text from X-ray crystallographic scattering data. The electron density map corresponds with part of the active site of an enzyme LysU (see next Fig. 6.19 Chapters 7 and 8) from the organism Escherichia coli. This electron density map has been "fitted" with the primary sequence polypeptide chain of LysU (colour code - carbon yellow oxygen red nitrogen blue). Once an electron density map has been determined, fitting of the known primary sequence of the biological macromolecule to the electron density map is the final stage that leads to a defined three-dimensional structure (from Onesti et al., 1995, Fig. 9).

Yang, X.-Y.H., Schulz, H., Elzinga, M. Yang, S.-Y. (1991) Biochemistry 30, 6788-6795. Nucleotide sequence of the promoter mAfadB gene of WtcfadBA operon and primary structure of the multifunctional fatty acid oxidation protein from Escherichia coli. 

Cr, and Cd, which in some cases bind ligands such as cyanide, thiols, and carbon monoxide. The mutant forms of the ferredoxin that have been studied have focused mainly on the residues that bind the iron-sulfur cluster. P. furiosus ferredoxin is also the primary electron acceptor for a variety of oxidoreductase-type enzymes in this organism, and the structure of an oxidoreductase-Fd complex has been reported. In this chapter we describe the purification of ferredoxin from P. furiosus, and the purification of the recombinant protein from Escherichia coli, together with several mutant forms. Some of the methods that have been developed in characterizing this protein are also described. The use of NMR spectroscopy to study P. furiosus ferredoxin is described elsewhere in this volume. ... 

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