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1jxa

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|SITE=
|SITE=
|LIGAND= <scene name='pdbligand=G6Q:GLUCOSE-6-PHOSPHATE'>G6Q</scene>
|LIGAND= <scene name='pdbligand=G6Q:GLUCOSE-6-PHOSPHATE'>G6Q</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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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1gdo|1gdo]], [[1moq|1moq]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jxa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jxa OCA], [http://www.ebi.ac.uk/pdbsum/1jxa PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jxa RCSB]</span>
}}
}}
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[[Category: Obmolova, G.]]
[[Category: Obmolova, G.]]
[[Category: Teplyakov, A.]]
[[Category: Teplyakov, A.]]
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[[Category: G6Q]]
 
[[Category: ammonia channel]]
[[Category: ammonia channel]]
[[Category: beta-sandwich]]
[[Category: beta-sandwich]]
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[[Category: nucleotide-binding fold]]
[[Category: nucleotide-binding fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:09:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:40:17 2008''

Revision as of 18:40, 30 March 2008


PDB ID 1jxa

Drag the structure with the mouse to rotate
, resolution 3.1Å
Ligands:
Activity: Glutamine--fructose-6-phosphate transaminase (isomerizing), with EC number 2.6.1.16
Related: 1gdo, 1moq


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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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