2bpl
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2bpl.gif|left|200px]] | [[Image:2bpl.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2bpl", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_2bpl| PDB=2bpl | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''E.COLI GLUCOSAMINE-6P SYNTHASE IN COMPLEX WITH FRUCTOSE-6P''' | '''E.COLI GLUCOSAMINE-6P SYNTHASE IN COMPLEX WITH FRUCTOSE-6P''' | ||
| Line 24: | Line 21: | ||
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] | 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: Single protein]] | [[Category: Single protein]] | ||
[[Category: Golinelli-Pimpaneau, B.]] | [[Category: Golinelli-Pimpaneau, B.]] | ||
[[Category: Mouilleron, S.]] | [[Category: Mouilleron, S.]] | ||
| - | [[Category: | + | [[Category: Amidotransferase]] |
| - | [[Category: | + | [[Category: Ammonia channeling]] |
| - | [[Category: | + | [[Category: Fructose 6-phosphate]] |
| - | [[Category: | + | [[Category: Glucosamine 6-phosphate synthase]] |
| - | [[Category: | + | [[Category: Glutamine amidotransferase]] |
| - | [[Category: | + | [[Category: N terminal nucleophile]] |
| - | [[Category: | + | [[Category: Transferase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:37:06 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:37, 3 May 2008
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 Page seeded by OCA on Sat May 3 20:37:06 2008
