1hwu: Difference between revisions

Revision as of 14:05, 21 February 2008

STRUCTURE OF PII PROTEIN FROM HERBASPIRILLUM SEROPEDICAE

OverviewOverview

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 beta 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.

About this StructureAbout this Structure

1HWU is a Single protein structure of sequence from Herbaspirillum seropedicae. Full crystallographic information is available from OCA.

ReferenceReference

Herbaspirillum seropedicae signal transduction protein PII is structurally similar to the enteric GlnK., Machado Benelli E, Buck M, Polikarpov I, Maltempi de Souza E, Cruz LM, Pedrosa FO, Eur J Biochem. 2002 Jul;269(13):3296-303. PMID:12084071

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OCA

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-[[Image:1hwu.gif|left|200px]]<br /><applet load="1hwu" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1hwu, resolution 2.1&Aring;" />
 '''STRUCTURE OF PII PROTEIN FROM HERBASPIRILLUM SEROPEDICAE'''<br />
 ==Overview==
-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 beta 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.
+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 beta 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.
 ==About this Structure==
-HWU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Herbaspirillum_seropedicae Herbaspirillum seropedicae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HWU OCA].
+HWU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Herbaspirillum_seropedicae Herbaspirillum seropedicae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HWU OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Herbaspirillum seropedicae]]
 [[Category: Single protein]]
-[[Category: Benelli, E.M.]]
+[[Category: Benelli, E M.]]
 [[Category: Buck, M.]]
-[[Category: Cruz, L.M.]]
+[[Category: Cruz, L M.]]
-[[Category: Pedrosa, F.O.]]
+[[Category: Pedrosa, F O.]]
 [[Category: Polikarpov, I.]]
-[[Category: Souza, E.M.De.]]
+[[Category: Souza, E M.De.]]
 [[Category: beta-alpha-beta motif]]
 [[Category: herbaspirillum seropedicae pii]]
 [[Category: signal transduction protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:12:01 2007''
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