TAILIEUCHUNG - Báo cáo Y học: Herbaspirillum seropedicae signal transduction protein PII is structurally similar to the enteric GlnK

PII-like proteins are signal transduction proteins found in bacteria, archaea and eukaryotes. They mediate a variety of cellular responses. A second PII-like protein, called GlnK, has been found in several organisms. In the diazotroph Herbaspirillum seropedicae, PII protein is involved in sensing nitrogen levels and controlling nitrogen fixation genes. In this work, the crystal structure of the unliganded H. seropedicae PII was solved by X-ray diffraction. H. seropedicae PII has a Gly residue, Gly108 preceding Pro109 and the main-chain forms a b turn. . | Eur. J. Biochem. 269 3296-3303 2002 FEBS 2002 doi Herbaspirillum seropedicae signal transduction protein PII is structurally similar to the enteric GlnK Elaine Machado Benelli1 Martin Buck2 Igor Polikarpov3 Emanuel Maltempi de Souza1 Leonardo M. Cruz1 and Fabio O. Pedrosa1 1 Department of Biochemistry Universidade Federal do Parana Curitiba Brazil -Department of Biological Science Imperial College of Science Technology Medicine Sir Alexander Fleming Building Imperial College Road London UK 3Laboratorio Nacional de Luz Sincrotron Campinas Brazil PII-like proteins are signal transduction proteins found in bacteria archaea and eukaryotes. They mediate a variety of cellular responses. A second PII-like protein called GlnK has been found in several organisms. In the diazotroph Herbaspirillum seropedicae PII protein is involved in sensing nitrogen levels and controlling nitrogen fixation genes. In this work the crystal structure of the unliganded H. sero-pedicae PII was solved by X-ray diffraction. H. seropedicae PII has a Gly residue Gly108 preceding Pro109 and the main-chain forms a b turn. The glycine at position 108 allows a bend in the C-terminal main-chain thereby modifying the surface of the cleft between monomers and potentially changing function. The structure suggests that the C-terminal region of PII proteins may be involved in specificity of function and nonenteric diazotrophs are found to have the C-terminal consensus XGXDAX 107-112 . We are also proposing binding sites for ATP and 2-oxoglutarate based on the structural alignment of PII with PII-ATP GlnK-ATP 5-carboxymethyl-2-hydroxymuconate isomerase and 4-oxalocrotonate tautomerase bound to the inhibitor 2-oxo-3-pentynoate. Keywords nitrogen regulation PII X-ray structure crystal packing Herbaspirillum seropedicae GlnK. Control of nitrogen metabolism in many bacteria utilizes a conserved mechanism of intracellular signalling to regulate patterns of gene expression and .

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