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1hwu
From Proteopedia
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(New page: 200px<br /><applet load="1hwu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hwu, resolution 2.1Å" /> '''STRUCTURE OF PII PROT...)
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Revision as of 01:04, 25 November 2007
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STRUCTURE OF PII PROTEIN FROM HERBASPIRILLUM SEROPEDICAE
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.
About this Structure
1HWU is a Single protein structure of sequence from Herbaspirillum seropedicae. Full crystallographic information is available from OCA.
Reference
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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