1a6j

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[[Image:1a6j.gif|left|200px]]<br /><applet load="1a6j" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1a6j.gif|left|200px]]<br /><applet load="1a6j" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1a6j, resolution 2.35&Aring;" />
caption="1a6j, resolution 2.35&Aring;" />
'''NITROGEN REGULATORY BACTERIAL PROTEIN IIA-NITROGEN'''<br />
'''NITROGEN REGULATORY BACTERIAL PROTEIN IIA-NITROGEN'''<br />
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==About this Structure==
==About this Structure==
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1A6J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and BME as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Protein-N(pi)-phosphohistidine--sugar_phosphotransferase Protein-N(pi)-phosphohistidine--sugar phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.69 2.7.1.69] Known structural/functional Sites: <scene name='pdbsite=PH1:By Comparison w. Iia Enzymes, This Is The Phosphorylatio ...'>PH1</scene> and <scene name='pdbsite=PH2:By Comparison w. Iia Enzymes, This Is The Phosphorylatio ...'>PH2</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A6J OCA].
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1A6J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Protein-N(pi)-phosphohistidine--sugar_phosphotransferase Protein-N(pi)-phosphohistidine--sugar phosphotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.69 2.7.1.69] Known structural/functional Sites: <scene name='pdbsite=PH1:By+Comparison+w.+Iia+Enzymes,+This+Is+The+Phosphorylatio+...'>PH1</scene> and <scene name='pdbsite=PH2:By+Comparison+w.+Iia+Enzymes,+This+Is+The+Phosphorylatio+...'>PH2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A6J OCA].
==Reference==
==Reference==
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[[Category: phosphotransferase system]]
[[Category: phosphotransferase system]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:10:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:29:21 2008''

Revision as of 07:29, 3 February 2008


1a6j, resolution 2.35Å

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NITROGEN REGULATORY BACTERIAL PROTEIN IIA-NITROGEN

Overview

The bacterial rpoN operon codes for sigma 54, which is the key sigma, factor that, under nitrogen starvation conditions, activates the, transcription of genes needed to assimilate ammonia and glutamate. The, rpoN operon contains several other open reading frames that are, cotranscribed with sigma 54. The product of one of these, the 17.9 kDa, protein IIANtr, is homologous to IIA proteins of the, phosphoenolpyruvate:sugar phosphotransferase (PTS) system. IIANtr, influences the transcription of sigma 54-dependent genes through an, unknown mechanism and may thereby provide a regulatory link between carbon, and nitrogen metabolism. Here we describe the 2.35 A X-ray structure of, Escherichia coli IIANtr. It is the first structure of a IIA enzyme from, the fructose-mannitol family of the PTS. The enzyme displays a novel fold, characterized by a central mixed parallel/anti-parallel beta-sheet, surrounded by six alpha-helices. The active site His73 is situated in a, shallow depression on the protein surface.

About this Structure

1A6J is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Protein-N(pi)-phosphohistidine--sugar phosphotransferase, with EC number 2.7.1.69 Known structural/functional Sites: and . Full crystallographic information is available from OCA.

Reference

The three-dimensional structure of the nitrogen regulatory protein IIANtr from Escherichia coli., Bordo D, van Monfort RL, Pijning T, Kalk KH, Reizer J, Saier MH Jr, Dijkstra BW, J Mol Biol. 1998 May 29;279(1):245-55. PMID:9636714

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