2bpl
From Proteopedia
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==Overview== | ==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 ... | + | 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== | ==About this Structure== | ||
| - | 2BPL is a | + | 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 F6R 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] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BPL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 12:42:16 2007'' |
Revision as of 10:36, 5 November 2007
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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 with F6R as ligand. Active as Glutamine--fructose-6-phosphate transaminase (isomerizing), with EC number 2.6.1.16 Structure known Active Site: AC1. 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
Page seeded by OCA on Mon Nov 5 12:42:16 2007
Categories: Escherichia coli | Glutamine--fructose-6-phosphate transaminase (isomerizing) | Single protein | Golinelli-Pimpaneau, B. | Mouilleron, S. | F6R | Amidotransferase | Ammonia channeling | Fructose 6-phosphate | Glucosamine 6-phosphate synthase | Glutamine amidotransferase | N terminal nucleophile | Transferase
