2bpl

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[[Image:2bpl.gif|left|200px]]<br /><applet load="2bpl" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2bpl.gif|left|200px]]
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caption="2bpl, resolution 2.05&Aring;" />
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'''E.COLI GLUCOSAMINE-6P SYNTHASE IN COMPLEX WITH FRUCTOSE-6P'''<br />
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{{Structure
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|PDB= 2bpl |SIZE=350|CAPTION= <scene name='initialview01'>2bpl</scene>, resolution 2.05&Aring;
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|SITE= <scene name='pdbsite=AC1:F6r+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=F6R:FRUCTOSE -6-PHOSPHATE'>F6R</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''E.COLI GLUCOSAMINE-6P SYNTHASE IN COMPLEX WITH FRUCTOSE-6P'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2BPL 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=F6R:'>F6R</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] Known structural/functional Site: <scene name='pdbsite=AC1:F6r+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BPL OCA].
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2BPL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BPL OCA].
==Reference==
==Reference==
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Glutamine binding opens the ammonia channel and activates glucosamine-6P synthase., Mouilleron S, Badet-Denisot MA, Golinelli-Pimpaneau B, J Biol Chem. 2006 Feb 17;281(7):4404-12. Epub 2005 Dec 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16339762 16339762]
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Glutamine binding opens the ammonia channel and activates glucosamine-6P synthase., Mouilleron S, Badet-Denisot MA, Golinelli-Pimpaneau B, J Biol Chem. 2006 Feb 17;281(7):4404-12. Epub 2005 Dec 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16339762 16339762]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Glutamine--fructose-6-phosphate transaminase (isomerizing)]]
[[Category: Glutamine--fructose-6-phosphate transaminase (isomerizing)]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:40:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:04:58 2008''

Revision as of 14:04, 20 March 2008

Image:2bpl.gif


PDB ID 2bpl

Drag the structure with the mouse to rotate
, resolution 2.05Å
Sites:
Ligands:
Activity: Glutamine--fructose-6-phosphate transaminase (isomerizing), with EC number 2.6.1.16
Coordinates: save as pdb, mmCIF, xml



E.COLI GLUCOSAMINE-6P SYNTHASE IN COMPLEX WITH FRUCTOSE-6P


Overview

Glucosamine-6P synthase catalyzes the synthesis of glucosamine-6P from fructose-6P and glutamine and uses a channel to transfer ammonia from its glutaminase to its synthase active site. X-ray structures of glucosamine-6P synthase have been determined at 2.05 Angstroms resolution in the presence of fructose-6P and at 2.35 Angstroms resolution in the presence of fructose-6P and 6-diazo-5-oxo-L-norleucine, a glutamine affinity analog that covalently modifies the N-terminal catalytic cysteine, therefore mimicking the gamma-glutamyl-thioester intermediate formed during hydrolysis of glutamine. The fixation of the glutamine analog activates the enzyme through several major structural changes: 1) the closure of a loop to shield the glutaminase site accompanied by significant domain hinging, 2) the activation of catalytic residues involved in glutamine hydrolysis, i.e. the alpha-amino group of Cys-1 and Asn-98 that is positioned to form the oxyanion hole, and 3) a 75 degrees rotation of the Trp-74 indole group that opens the ammonia channel.

About this Structure

2BPL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Glutamine binding opens the ammonia channel and activates glucosamine-6P synthase., Mouilleron S, Badet-Denisot MA, Golinelli-Pimpaneau B, J Biol Chem. 2006 Feb 17;281(7):4404-12. Epub 2005 Dec 9. PMID:16339762

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