1jxa

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(New page: 200px<br /><applet load="1jxa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jxa, resolution 3.1&Aring;" /> '''GLUCOSAMINE 6-PHOSPHA...)
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[[Image:1jxa.gif|left|200px]]<br /><applet load="1jxa" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jxa.gif|left|200px]]<br /><applet load="1jxa" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jxa, resolution 3.1&Aring;" />
caption="1jxa, resolution 3.1&Aring;" />
'''GLUCOSAMINE 6-PHOSPHATE SYNTHASE WITH GLUCOSE 6-PHOSPHATE'''<br />
'''GLUCOSAMINE 6-PHOSPHATE SYNTHASE WITH GLUCOSE 6-PHOSPHATE'''<br />
==Overview==
==Overview==
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Glucosamine-6-phosphate synthase catalyses the first and rate-limiting, step in hexosamine metabolism, converting fructose 6-phosphate into, glucosamine 6-phosphate in the presence of glutamine. The crystal, structure of the Escherichia coli enzyme reveals the domain organisation, of the homodimeric molecule. The 18 A hydrophobic channel sequestered from, the solvent connects the glutaminase and isomerase active sites, and, provides a means of ammonia transfer from glutamine to sugar phosphate., The C-terminal decapeptide sandwiched between the two domains plays a, central role in the transfer. Based on the structure, a mechanism of, enzyme action and self-regulation is proposed. It involves large domain, movements triggered by substrate binding that lead to the formation of the, channel.
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Glucosamine-6-phosphate synthase catalyses the first and rate-limiting step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate in the presence of glutamine. The crystal structure of the Escherichia coli enzyme reveals the domain organisation of the homodimeric molecule. The 18 A hydrophobic channel sequestered from the solvent connects the glutaminase and isomerase active sites, and provides a means of ammonia transfer from glutamine to sugar phosphate. The C-terminal decapeptide sandwiched between the two domains plays a central role in the transfer. Based on the structure, a mechanism of enzyme action and self-regulation is proposed. It involves large domain movements triggered by substrate binding that lead to the formation of the channel.
==About this Structure==
==About this Structure==
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1JXA 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 G6Q as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutamine--fructose-6-phosphate_transaminase_(isomerizing) Glutamine--fructose-6-phosphate transaminase (isomerizing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.16 2.6.1.16] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JXA OCA].
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1JXA 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=G6Q:'>G6Q</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutamine--fructose-6-phosphate_transaminase_(isomerizing) Glutamine--fructose-6-phosphate transaminase (isomerizing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.16 2.6.1.16] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JXA OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Badet, B.]]
[[Category: Badet, B.]]
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[[Category: Badet-Denisot, M.A.]]
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[[Category: Badet-Denisot, M A.]]
[[Category: Obmolova, G.]]
[[Category: Obmolova, G.]]
[[Category: Teplyakov, A.]]
[[Category: Teplyakov, A.]]
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[[Category: nucleotide-binding fold]]
[[Category: nucleotide-binding fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:39:33 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:27:45 2008''

Revision as of 11:27, 21 February 2008


1jxa, resolution 3.1Å

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GLUCOSAMINE 6-PHOSPHATE SYNTHASE WITH GLUCOSE 6-PHOSPHATE

Overview

Glucosamine-6-phosphate synthase catalyses the first and rate-limiting step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate in the presence of glutamine. The crystal structure of the Escherichia coli enzyme reveals the domain organisation of the homodimeric molecule. The 18 A hydrophobic channel sequestered from the solvent connects the glutaminase and isomerase active sites, and provides a means of ammonia transfer from glutamine to sugar phosphate. The C-terminal decapeptide sandwiched between the two domains plays a central role in the transfer. Based on the structure, a mechanism of enzyme action and self-regulation is proposed. It involves large domain movements triggered by substrate binding that lead to the formation of the channel.

About this Structure

1JXA is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Glutamine--fructose-6-phosphate transaminase (isomerizing), with EC number 2.6.1.16 Full crystallographic information is available from OCA.

Reference

Channeling of ammonia in glucosamine-6-phosphate synthase., Teplyakov A, Obmolova G, Badet B, Badet-Denisot MA, J Mol Biol. 2001 Nov 9;313(5):1093-102. PMID:11700065

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